document_title: Electron transport chain

question_text: nadh and fadh2 are used to transport what item used in cellular respiration

text: Electron transport chain

text: Background[edit]

text: The electron transport chain consists of a spatially separated series of redox reactions in which electrons are transferred from a donor molecule to an acceptor molecule. The underlying force driving these reactions is the Gibbs free energy of the reactants and products. The Gibbs free energy is the energy available ("free") to do work. Any reaction that decreases the overall Gibbs free energy of a system is thermodynamically spontaneous.

text: The function of the electron transport chain is to produce a transmembrane proton electrochemical gradient as a result of the redox reactions.[1] If protons flow back through the membrane, they enable mechanical work, such as rotating bacterial flagella. ATP synthase, an enzyme highly conserved among all domains of life, converts this mechanical work into chemical energy by producing ATP,[2] which powers most cellular reactions. A small amount of ATP is available from substrate-level phosphorylation, for example, in glycolysis. In most organisms the majority of ATP is generated in electron transport chains, while only some obtain ATP by fermentation.[citation needed]

text: In mitochondria[edit]

text: Most eukaryotic cells have mitochondria, which produce ATP from products of the citric acid cycle, fatty acid oxidation, and amino acid oxidation. At the mitochondrial inner membrane, electrons from NADH and FADH2 pass through the electron transport chain to oxygen, which is reduced to water. The electron transport chain comprises an enzymatic series of electron donors and acceptors. Each electron donor will pass electrons to a more electronegative acceptor, which in turn donates these electrons to another acceptor, a process that continues down the series until electrons are passed to oxygen, the most electronegative and terminal electron acceptor in the chain. Passage of electrons between donor and acceptor releases energy, which is used to generate a proton gradient across the mitochondrial membrane by actively "pumping" protons into the intermembrane space, producing a thermodynamic state that has the potential to do work. The entire process is called oxidative phosphorylation, since ADP is phosphorylated to ATP using the energy of hydrogen oxidation in many steps.

text: A small percentage of electrons do not complete the whole series and instead directly leak to oxygen, resulting in the formation of the free-radical superoxide, a highly reactive molecule that contributes to oxidative stress and has been implicated in a number of diseases and aging.

text: Mitochondrial redox carriers[edit]

text: Energy obtained through the transfer of electrons down the ETC is used to pump protons from the mitochondrial matrix into the intermembrane space, creating an electrochemical proton gradient (ΔpH) across the inner mitochondrial membrane (IMM). This proton gradient is largely but not exclusively responsible for the mitochondrial membrane potential (ΔΨM). It allows ATP synthase to use the flow of H+ through the enzyme back into the matrix to generate ATP from adenosine diphosphate (ADP) and inorganic phosphate. Complex I (NADH coenzyme Q reductase; labeled I) accepts electrons from the Krebs cycle electron carrier nicotinamide adenine dinucleotide (NADH), and passes them to coenzyme Q (ubiquinone; labeled Q), which also receives electrons from complex II (succinate dehydrogenase; labeled II). Q passes electrons to complex III (cytochrome bc1 complex; labeled III), which passes them to cytochrome c (cyt c). Cyt c passes electrons to Complex IV (cytochrome c oxidase; labeled IV), which uses the electrons and hydrogen ions to reduce molecular oxygen to water.

text: Four membrane-bound complexes have been identified in mitochondria. Each is an extremely complex transmembrane structure that is embedded in the inner membrane. Three of them are proton pumps. The structures are electrically connected by lipid-soluble electron carriers and water-soluble electron carriers. The overall electron transport chain:

text: Complex I[edit]

text: In Complex I (NADH:ubiquinone oxidoreductase, NADH-CoQ reductase, or NADH dehydrogenase; EC 1.6.5.3), two electrons are removed from NADH and ultimately transferred to a lipid-soluble carrier, ubiquinone (UQ). The reduced product, ubiquinol (UQH2), freely diffuses within the membrane, and Complex I translocates four protons (H+) across the membrane, thus producing a proton gradient. Complex I is one of the main sites at which premature electron leakage to oxygen occurs, thus being one of the main sites of production of superoxide.[3]

text: The pathway of electrons is as follows:

text: NADH is oxidized to NAD+, by reducing Flavin mononucleotide to FMNH2 in one two-electron step. FMNH2 is then oxidized in two one-electron steps, through a semiquinone intermediate. Each electron thus transfers from the FMNH2 to an Fe-S cluster, from the Fe-S cluster to ubiquinone (Q). Transfer of the first electron results in the free-radical (semiquinone) form of Q, and transfer of the second electron reduces the semiquinone form to the ubiquinol form, QH2. During this process, four protons are translocated from the mitochondrial matrix to the intermembrane space. [4] As the electrons become continuously oxidized and reduced throughout the complex an electron current is produced along the 180 Angstrom width of the complex within the membrane. This current powers the active transport of four protons to the intermembrane space per two electrons from NADH.[5]

text: This complex is inhibited by Alkylguanides (Example : Guanethidine), Rotenone, Barbiturates, Chlorpromazine, Piericidin.

text: Complex II[edit]

text: In Complex II (succinate dehydrogenase or succinate-CoQ reductase; EC 1.3.5.1) additional electrons are delivered into the quinone pool (Q) originating from succinate and transferred (via flavin adenine dinucleotide (FAD)) to Q. Complex II consists of four protein subunits: succinate dehydrogenase, (SDHA); succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, (SDHB); succinate dehydrogenase complex subunit C, (SDHC) and succinate dehydrogenase complex, subunit D, (SDHD). Other electron donors (e.g., fatty acids and glycerol 3-phosphate) also direct electrons into Q (via FAD). Complex 2 is a parallel electron transport pathway to complex 1, but unlike complex 1, no protons are transported to the intermembrane space in this pathway. Therefore, the pathway through complex 2 contributes less energy to the overall electron transport chain process.

text: This complex is inhibited by Carboxin.

text: Complex III[edit]

text:
In Complex III (cytochrome bc1 complex or CoQH2-cytochrome c reductase; EC 1.10.2.2), the Q-cycle contributes to the proton gradient by an asymmetric absorption/release of protons. Two electrons are removed from QH2 at the QO site and sequentially transferred to two molecules of cytochrome c, a water-soluble electron carrier located within the intermembrane space. The two other electrons sequentially pass across the protein to the Qi site where the quinone part of ubiquinone is reduced to quinol. A proton gradient is formed by one quinol (

2

H

2

+

e

−

{\displaystyle {\ce {2H+2e-}}}

) oxidations at the Qo site to form one quinone (

2

H

2

+

e

−

{\displaystyle {\ce {2H+2e-}}}

) at the Qi site. (in total four protons are translocated: two protons reduce quinone to quinol and two protons are released from two ubiquinol molecules).

text: When electron transfer is reduced (by a high membrane potential or respiratory inhibitors such as antimycin A), Complex III may leak electrons to molecular oxygen, resulting in superoxide formation.

text: This complex is inhibited by British Antilewisite(BAL), Napthoquinone and Antimycin.

text: Complex IV[edit]

text: In Complex IV (cytochrome c oxidase; EC 1.9.3.1), sometimes called cytochrome AA3, four electrons are removed from four molecules of cytochrome c and transferred to molecular oxygen (O2), producing two molecules of water. At the same time, eight protons are removed from the mitochondrial matrix (although only four are translocated across the membrane), contributing to the proton gradient. The activity of cytochrome c oxidase is inhibited by cyanide, carbon monoxide, azide, hydrogen sulphide(H2S).

text: Coupling with oxidative phosphorylation[edit]

text:
According to the chemiosmotic coupling hypothesis, proposed by Nobel Prize in Chemistry winner Peter D. Mitchell, the electron transport chain and oxidative phosphorylation are coupled by a proton gradient across the inner mitochondrial membrane. The efflux of protons from the mitochondrial matrix creates an electrochemical gradient (proton gradient). This gradient is used by the FOF1 ATP synthase complex to make ATP via oxidative phosphorylation. ATP synthase is sometimes described as Complex V of the electron transport chain.[6] The FO component of ATP synthase acts as an ion channel that provides for a proton flux back into the mitochondrial matrix. It is composed of a, b and c subunits. Protons in the inter-membranous space of mitochondria first enters the ATP synthase complex through a subunit channel. Then protons move to the c subunits.[7] The number of c subunits it has determines how many protons it will require to make the FO turn one full revolution. For example, in humans, there are 8 c subunits, thus 8 protons are required.[8] After c subunits, protons finally enters matrix using a subunit channel that opens into the mitochondrial matrix.[7] This reflux releases free energy produced during the generation of the oxidized forms of the electron carriers (NAD+ and Q). The free energy is used to drive ATP synthesis, catalyzed by the F1 component of the complex.[9]
Coupling with oxidative phosphorylation is a key step for ATP production. However, in specific cases, uncoupling the two processes may be biologically useful. The uncoupling protein, thermogenin—present in the inner mitochondrial membrane of brown adipose tissue—provides for an alternative flow of protons back to the inner mitochondrial matrix. Thyroxine is also a natural uncoupler. This alternative flow results in thermogenesis rather than ATP production.[10] Synthetic uncouplers (e.g., 2,4-dinitrophenol, 2,4-dinitrocresol, CCCP) also exist, and can be lethal at high doses.[citation needed]

text: Summary[edit]

text: In the mitochondrial electron transport chain electrons move from an electron donor (NADH or QH2) to a terminal electron acceptor (O2) via a series of redox reactions. These reactions are coupled to the creation of a proton gradient across the mitochondrial inner membrane. There are three proton pumps: I, III, and IV. The resulting transmembrane proton gradient is used to make ATP via ATP synthase.

text: The reactions catalyzed by Complex I and Complex III work roughly at equilibrium. This means that these reactions are readily reversible, by increasing the concentration of the products relative to the concentration of the reactants (for example, by increasing the proton gradient). ATP synthase is also readily reversible. Thus ATP can be used to build a proton gradient, which in turn can be used to make NADH. This process of reverse electron transport is important in many prokaryotic electron transport chains.[11]

text: In bacteria[edit]

text: In eukaryotes, NADH is the most important electron donor. The associated electron transport chain is

text: NADH → Complex I → Q → Complex III → cytochrome c → Complex IV → O2 where Complexes I, III and IV are proton pumps, while Q and cytochrome c are mobile electron carriers. The electron acceptor is molecular oxygen.

text: In prokaryotes (bacteria and archaea) the situation is more complicated, because there are several different electron donors and several different electron acceptors. The generalized electron transport chain in bacteria is:

text: Note that electrons can enter the chain at three levels: at the level of a dehydrogenase, at the level of the quinone pool, or at the level of a mobile cytochrome electron carrier. These levels correspond to successively more positive redox potentials, or to successively decreased potential differences relative to the terminal electron acceptor. In other words, they correspond to successively smaller Gibbs free energy changes for the overall redox reaction Donor → Acceptor.

text: Individual bacteria use multiple electron transport chains, often simultaneously. Bacteria can use a number of different electron donors, a number of different dehydrogenases, a number of different oxidases and reductases, and a number of different electron acceptors. For example, E. coli (when growing aerobically using glucose as an energy source) uses two different NADH dehydrogenases and two different quinol oxidases, for a total of four different electron transport chains operating simultaneously.

text: A common feature of all electron transport chains is the presence of a proton pump to create a transmembrane proton gradient. Bacterial electron transport chains may contain as many as three proton pumps, like mitochondria, or they may contain only one or two. They always contain at least one proton pump.

text: Electron donors[edit]

text: In the present day biosphere, the most common electron donors are organic molecules. Organisms that use organic molecules as an energy source are called organotrophs. Organotrophs (animals, fungi, protists) and phototrophs (plants and algae) constitute the vast majority of all familiar life forms.

text: Some prokaryotes can use inorganic matter as an energy source. Such an organism is called a lithotroph ("rock-eater"). Inorganic electron donors include hydrogen, carbon monoxide, ammonia, nitrite, sulfur, sulfide, manganese oxide, and ferrous iron. Lithotrophs have been found growing in rock formations thousands of meters below the surface of Earth. Because of their volume of distribution, lithotrophs may actually outnumber organotrophs and phototrophs in our biosphere.

text: The use of inorganic electron donors as an energy source is of particular interest in the study of evolution. This type of metabolism must logically have preceded the use of organic molecules as an energy source.

text: Dehydrogenases[edit]

text: Bacteria can use a number of different electron donors. When organic matter is the energy source, the donor may be NADH or succinate, in which case electrons enter the electron transport chain via NADH dehydrogenase (similar to Complex I in mitochondria) or succinate dehydrogenase (similar to Complex II). Other dehydrogenases may be used to process different energy sources: formate dehydrogenase, lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, H2 dehydrogenase (hydrogenase), etc. Some dehydrogenases are also proton pumps; others funnel electrons into the quinone pool. Most dehydrogenases show induced expression in the bacterial cell in response to metabolic needs triggered by the environment in which the cells grow.[citation needed]

text: Quinone carriers[edit]

text: Quinones are mobile, lipid-soluble carriers that shuttle electrons (and protons) between large, relatively immobile macromolecular complexes embedded in the membrane. Bacteria use ubiquinone (the same quinone that mitochondria use) and related quinones such as menaquinone. Another name for ubiquinone is Coenzyme Q10.

text: Proton pumps[edit]

text: A proton pump is any process that creates a proton gradient across a membrane. Protons can be physically moved across a membrane; this is seen in mitochondrial Complexes I and IV. The same effect can be produced by moving electrons in the opposite direction. The result is the disappearance of a proton from the cytoplasm and the appearance of a proton in the periplasm. Mitochondrial Complex III uses this second type of proton pump, which is mediated by a quinone (the Q cycle).

text: Some dehydrogenases are proton pumps; others are not. Most oxidases and reductases are proton pumps, but some are not. Cytochrome bc1 is a proton pump found in many, but not all, bacteria (it is not found in E. coli). As the name implies, bacterial bc1 is similar to mitochondrial bc1 (Complex III).

text: Proton pumps are the heart of the electron transport process. They produce the transmembrane electrochemical gradient that enables ATP Synthase to synthesize ATP.

text: Cytochrome electron carriers[edit]

text: Cytochromes are pigments that contain iron. They are found in two very different environments.

text: Some cytochromes are water-soluble carriers that shuttle electrons to and from large, immobile macromolecular structures imbedded in the membrane. The mobile cytochrome electron carrier in mitochondria is cytochrome c. Bacteria use a number of different mobile cytochrome electron carriers.

text: Other cytochromes are found within macromolecules such as Complex III and Complex IV. They also function as electron carriers, but in a very different, intramolecular, solid-state environment.

text: Electrons may enter an electron transport chain at the level of a mobile cytochrome or quinone carrier. For example, electrons from inorganic electron donors (nitrite, ferrous iron, etc.) enter the electron transport chain at the cytochrome level. When electrons enter at a redox level greater than NADH, the electron transport chain must operate in reverse to produce this necessary, higher-energy molecule.

text: Terminal oxidases and reductases[edit]

text: When bacteria grow in aerobic environments, the terminal electron acceptor (O2) is reduced to water by an enzyme called an oxidase. When bacteria grow in anaerobic environments, the terminal electron acceptor is reduced by an enzyme called a reductase.

text: In mitochondria the terminal membrane complex (Complex IV) is cytochrome oxidase. Aerobic bacteria use a number of different terminal oxidases. For example, E. coli does not have a cytochrome oxidase or a bc1 complex. Under aerobic conditions, it uses two different terminal quinol oxidases (both proton pumps) to reduce oxygen to water.

text: Anaerobic bacteria, which do not use oxygen as a terminal electron acceptor, have terminal reductases individualized to their terminal acceptor. For example, E. coli can use fumarate reductase, nitrate reductase, nitrite reductase, DMSO reductase, or trimethylamine-N-oxide reductase, depending on the availability of these acceptors in the environment.

text: Most terminal oxidases and reductases are inducible. They are synthesized by the organism as needed, in response to specific environmental conditions.

text: Electron acceptors[edit]

text: Just as there are a number of different electron donors (organic matter in organotrophs, inorganic matter in lithotrophs), there are a number of different electron acceptors, both organic and inorganic. If oxygen is available, it is invariably used as the terminal electron acceptor, because it generates the greatest Gibbs free energy change and produces the most energy.[citation needed]

text: In anaerobic environments, different electron acceptors are used, including nitrate, nitrite, ferric iron, sulfate, carbon dioxide, and small organic molecules such as fumarate.

text: Since electron transport chains are redox processes, they can be described as the sum of two redox pairs. For example, the mitochondrial electron transport chain can be described as the sum of the NAD+/NADH redox pair and the O2/H2O redox pair. NADH is the electron donor and O2 is the electron acceptor.

text: Not every donor-acceptor combination is thermodynamically possible. The redox potential of the acceptor must be more positive than the redox potential of the donor. Furthermore, actual environmental conditions may be far different from standard conditions (1 molar concentrations, 1 atm partial pressures, pH = 7), which apply to standard redox potentials. For example, hydrogen-evolving bacteria grow at an ambient partial pressure of hydrogen gas of 10−4 atm. The associated redox reaction, which is thermodynamically favorable in nature, is thermodynamic impossible under "standard" conditions.[citation needed]

text: Summary[edit]

text: Bacterial electron transport pathways are, in general, inducible. Depending on their environment, bacteria can synthesize different transmembrane complexes and produce different electron transport chains in their cell membranes. Bacteria select their electron transport chains from a DNA library containing multiple possible dehydrogenases, terminal oxidases and terminal reductases. The situation is often summarized by saying that electron transport chains in bacteria are branched, modular, and inducible.

text: Photosynthetic[edit]

text: In oxidative phosphorylation, electrons are transferred from a low-energy electron donor (e.g., NADH) to an acceptor (e.g., O2) through an electron transport chain. In photophosphorylation, the energy of sunlight is used to create a high-energy electron donor and an electron acceptor. Electrons are then transferred from the donor to the acceptor through another electron transport chain.

text: Photosynthetic electron transport chains have many similarities to the oxidative chains discussed above. They use mobile, lipid-soluble carriers (quinones) and mobile, water-soluble carriers (cytochromes, etc.). They also contain a proton pump. It is remarkable that the proton pump in all photosynthetic chains resembles mitochondrial Complex III.

text: Photosynthetic electron transport chains are discussed in greater detail in the articles Photophosphorylation, Photosynthesis, Photosynthetic reaction center and Light-dependent reaction.

text: Summary[edit]

text: Electron transport chains are redox reactions that transfer electrons from an electron donor to an electron acceptor. The transfer of electrons is coupled to the translocation of protons across a membrane, producing a proton gradient. The proton gradient is used to produce useful work. About 30 work units are produced per electron transport.


document_title: List of the verified oldest people

question_text: how old was the oldest person ever to live on earth

root

text: List of the verified oldest people

text: This is a list of the 100 verified oldest people, arranged in descending order of each individual's age in years and days. A year typically refers to a calendar year, the time between two dates of the same name. However, years can be of different lengths due to the presence or absence of a leap day within the year, or to the conversion of dates from one calendar to another.

tag: p

text: The oldest person ever whose age has been verified is Jeanne Calment (1875–1997) of France, who died at the age of 122 years, 164 days.

text: There are five living people on this list, all of whom are women and the oldest of whom is Kane Tanaka of Japan, aged 115 years, 239 days.

text: Since all the people on this list have lived past the age of 110, all of them have been, or still are, supercentenarians.

text: 100 verified oldest people[edit]

text:
Deceased
  Living

†^  denotes age at death, or, if living, age as of  today, 29 August 2018

text:
Rank

Name

Sex

Birth date

Death date

Age [†]

Place of death or residence

1

Jeanne Calment[1]

F

21 February 1875

4 August 1997

122 years, 164 days

France

2

Sarah Knauss[2]

F

24 September 1880

30 December 1999

119 years, 97 days

United States

3

Nabi Tajima[3]

F

4 August 1900

21 April 2018

117 years, 260 days

Japan

4

Lucy Hannah[4]

F

16 July 1875

21 March 1993

117 years, 248 days

United States

5

Marie-Louise Meilleur[5]

F

29 August 1880

16 April 1998

117 years, 230 days

Canada

6

Violet Brown[3]

F

10 March 1900

15 September 2017

117 years, 189 days

Jamaica

7

Emma Morano[3][6]

F

29 November 1899

15 April 2017

117 years, 137 days

Italy

8

Chiyo Miyako[3][7][8]

F

2 May 1901

22 July 2018

117 years, 81 days

Japan

9

Misao Okawa[3]

F

5 March 1898

1 April 2015

117 years, 27 days

Japan

10

María Capovilla[9]

F

14 September 1889

27 August 2006

116 years, 347 days

Ecuador

11

Susannah Mushatt Jones[3]

F

6 July 1899

12 May 2016

116 years, 311 days

United States

12

Gertrude Weaver[3]

F

4 July 1898

6 April 2015

116 years, 276 days

United States

13

Tane Ikai[10]

F

18 January 1879

12 July 1995

116 years, 175 days

Japan

14

Elizabeth Bolden[11]

F

15 August 1890

11 December 2006

116 years, 118 days

United States

15

Besse Cooper[3]

F

26 August 1896

4 December 2012

116 years, 100 days

United States

16

Jiroemon Kimura[3]

M

19 April 1897

12 June 2013

116 years, 54 days

Japan

17

Ana María Vela Rubio[3]

F

29 October 1901

15 December 2017

116 years, 47 days

Spain

18

Giuseppina  Projetto[3]

F

30 May 1902

6 July 2018

116 years, 37 days

Italy

19

Jeralean Talley[3]

F

23 May 1899

17 June 2015

116 years, 25 days

United States

20

Maggie Barnes[12]

F

6 March 1882

19 January 1998

115 years, 319 days

United States

21

Dina Manfredini[3]

F

4 April 1897

17 December 2012

115 years, 257 days

United States[a]

22

Christian Mortensen[13]

M

16 August 1882

25 April 1998

115 years, 252 days

United States[b]

23

Kane Tanaka[3]

F

2 January 1903

Living[3]

7004422430000000000♠115 years, 239 days

Japan

24

Charlotte Hughes[14]

F

1 August 1877

17 March 1993

115 years, 228 days

United Kingdom

25

Edna Parker[15]

F

20 April 1893

26 November 2008

115 years, 220 days

United States

26

Mary Ann Rhodes[16]

F

12 August 1882

3 March 1998

115 years, 203 days

Canada

27

Anonymous of Tokyo[3]

F

15 March 1900

27 September 2015

115 years, 196 days

Japan

28

Margaret Skeete[17]

F

27 October 1878

7 May 1994

115 years, 192 days

United States

29

Bernice Madigan[18]

F

24 July 1899

3 January 2015

115 years, 163 days

United States

30

Maria Giuseppa Robucci[3]

F

20 March 1903

Living[3]

7004421660000000000♠115 years, 162 days

Italy

31

Gertrude Baines[19]

F

6 April 1894

11 September 2009

115 years, 158 days

United States

32

Emiliano Mercado del Toro[13]

M

21 August 1891

24 January 2007

115 years, 156 days

Puerto Rico

33

Bettie Wilson[20]

F

13 September 1890

13 February 2006

115 years, 153 days

United States

34

Julie Winnefred Bertrand[21]

F

16 September 1891

18 January 2007

115 years, 124 days

Canada

35

Maria de Jesus[22]

F

10 September 1893

2 January 2009

115 years, 114 days

Portugal

36

Marie Josephine Gaudette[3][23]

F

25 March 1902

13 July 2017

115 years, 110 days

Italy[c]

37

Susie Gibson[24]

F

31 October 1890

16 February 2006

115 years, 108 days

United States

38

Shimoe Akiyama[3]

F

19 May 1903

Living[3]

7004421060000000000♠115 years, 102 days

Japan

39

Augusta Holtz[25]

F

3 August 1871

21 October 1986

115 years, 79 days

United States[d]

40

Hendrikje van Andel-Schipper[26]

F

29 June 1890

30 August 2005

115 years, 62 days

Netherlands

41

Maude Farris-Luse[27]

F

21 January 1887

18 March 2002

115 years, 56 days

United States

42

Marie Brémont[28]

F

25 April 1886

6 June 2001

115 years, 42 days

France

43

Koto Okubo[29]

F

24 December 1897

12 January 2013

115 years, 19 days

Japan

44

Antonia Gerena Rivera[3]

F

19 May 1900

2 June 2015

115 years, 14 days

United States[e]

45

Chiyono Hasegawa[30]

F

20 November 1896

2 December 2011

115 years, 12 days

Japan

46

Annie Jennings[31]

F

12 November 1884

20 November 1999

115 years, 8 days

United Kingdom

47

Eva Morris[32]

F

8 November 1885

2 November 2000

114 years, 360 days

United Kingdom

48

Kama Chinen[33]

F

10 May 1895

2 May 2010

114 years, 357 days

Japan

49

Maria Gomes Valentim[34]

F

9 July 1896

21 June 2011

114 years, 347 days

Brazil

50

Mary Bidwell[35]

F

19 May 1881

25 April 1996

114 years, 342 days

United States

51

Mary Josephine Ray[36]

F

17 May 1895

7 March 2010

114 years, 294 days

United States[f]

52

Goldie Steinberg[3][37][38]

F

30 October 1900

16 August 2015

114 years, 290 days

United States[g]

53

Kiyoko Ishiguro[3]

F

4 March 1901

5 December 2015

114 years, 276 days

Japan

54

Maria do Couto Maia-Lopes[13]

F

24 October 1890

25 July 2005

114 years, 274 days

Portugal

Eudoxie Baboul[3]

F

1 October 1901

1 July 2016

114 years, 274 days

France (French Guiana)

56

Ramona Trinidad Iglesias-Jordan[39]

F

31 August 1889

29 May 2004

114 years, 272 days

Puerto Rico

57

Yukie Hino[3]

F

17 April 1902

13 January 2017

114 years, 271 days

Japan

58

Delphine Gibson[3]

F

17 August 1903

9 May 2018

114 years, 265 days

United States

59

Eugénie Blanchard[40]

F

16 February 1896

4 November 2010

114 years, 261 days

France (Saint Barthélemy)

60

Venere Pizzinato-Papo[41]

F

23 November 1896

2 August 2011

114 years, 252 days

Italy[h]

61

Neva Morris[42]

F

3 August 1895

6 April 2010

114 years, 246 days

United States

62

Hide Ohira[13]

F

15 September 1880

9 May 1995

114 years, 236 days

Japan

63

Blanche Cobb[43][44]

F

8 September 1900

1 May 2015

114 years, 235 days

United States

64

Ethel Lang[3]

F

27 May 1900

15 January 2015

114 years, 233 days

United Kingdom

65

Mathew Beard[13]

M

9 July 1870

16 February 1985

114 years, 222 days

United States

66

Yone Minagawa[45]

F

4 January 1893

13 August 2007

114 years, 221 days

Japan

67

María Antonia Castro[46]

F

10 June 1881

16 January 1996

114 years, 220 days

Spain

68

Carrie Lazenby[13]

F

9 February 1882

14 September 1996

114 years, 218 days

United States

Ura Koyama[47]

F

30 August 1890

5 April 2005

114 years, 218 days

Japan

70

Myrtle Dorsey[48]

F

22 November 1885

25 June 2000

114 years, 216 days

United States

71

Iso Nakamura[3]

F

23 April 1903

23 November 2017

114 years, 214 days

Japan

72

Anna Eliza Williams[49]

F

2 June 1873

27 December 1987

114 years, 208 days

United Kingdom

73

Walter Breuning[13]

M

21 September 1896

14 April 2011

114 years, 205 days

United States

74

Lucile Randon[3]

F

11 February 1904

Living[3]

7004418380000000000♠114 years, 199 days

France

75

Eunice Sanborn[50]

F

20 July 1896

31 January 2011

114 years, 195 days

United States

76

Grace Clawson[51]

F

15 November 1887

28 May 2002

114 years, 194 days

United States[i]

77

Mitsue Toyoda[3]

F

15 February 1902

25 August 2016

114 years, 192 days

Japan

78

Tase Matsunaga[52]

F

11 May 1884

18 November 1998

114 years, 191 days

Japan

79

Yukichi Chuganji[13]

M

23 March 1889

28 September 2003

114 years, 189 days

Japan

80

Kame Nakamura[53]

F

8 March 1898

12 September 2012

114 years, 188 days

Japan

81

Lydie Vellard[13]

F

18 March 1875

17 September 1989

114 years, 183 days

France

Wilhelmina Kott[54]

F

7 March 1880

6 September 1994

114 years, 183 days

United States

Adelina Domingues[55]

F

19 February 1888

21 August 2002

114 years, 183 days

United States[j]

84

Mitoyo Kawate[56]

F

15 May 1889

13 November 2003

114 years, 182 days

Japan

85

Charlotte Benkner[57]

F

16 November 1889

14 May 2004

114 years, 180 days

United States[k]

Camille Loiseau[58]

F

13 February 1892

12 August 2006

114 years, 180 days

France

87

Anne Primout[59]

F

5 October 1890

26 March 2005

114 years, 172 days

France[l]

88

Ettie Mae Greene[60]

F

8 September 1877

26 February 1992

114 years, 171 days

United States

89

Dominga Velasco[3]

F

12 May 1901

11 October 2015

114 years, 152 days

United States[m]

Shin Matsushita[3]

F

30 March 1904

Living[3]

7004417900000000000♠114 years, 152 days

Japan

91

Toshie Yorimitsu[3]

F

30 September 1901

28 February 2016

114 years, 151 days

Japan

92

Irene Frank[13]

F

1 October 1881

28 February 1996

114 years, 150 days

United States

93

Christina Cock[61]

F

25 December 1887

22 May 2002

114 years, 148 days

Australia[n]

94

Olivia Patricia Thomas[62]

F

29 June 1895

16 November 2009

114 years, 140 days

United States

95

Tae Ito[3]

F

11 July 1903

13 November 2017

114 years, 125 days

Japan

96

Anna Henderson[63]

F

5 March 1900

1 July 2014

114 years, 118 days

United States

97

Emma Verona Johnston[64]

F

6 August 1890

1 December 2004

114 years, 117 days

United States

Mamie Rearden[65]

F

7 September 1898

2 January 2013

114 years, 117 days

United States

99

Bettie Chatmon[13]

F

30 April 1884

16 August 1998

114 years, 108 days

United States

100

Odie Matthews[13]

F

28 December 1878

14 April 1993

114 years, 107 days

United States

tag: table

text:
a^  Manfredini was born in Italy.
b^  Mortensen was born in Denmark.
c^  Gaudette was born in the United States.
d^  Holtz was born in the German Empire; her birthplace is now in Poland.
e^  Gerena was born in Puerto Rico.
f^  Ray was born in Canada.
g^  Steinberg was born in Kishinev, then part of the Russian Empire. It is now the capital of Moldova.
h^  Pizzinato-Papo was born in Ala, which was then part of Austria-Hungary; it is now located in Italy.
i^  Clawson was born in the United Kingdom.
j^  Domingues was born in Cape Verde, at that time a colony of Portugal.
k^  Benkner was born in Germany.
l^  Primout was born in French Algeria; it is now Algeria.
m^  Velasco was born in Mexico.
n^  Cock was born in the former British colony Victoria, which is now part of Australia.