The functional catalytic unit involved in proton pumping by rat liver cytochrome-c reductase and by cytochrome-c oxidase.

AJ Moody; PR Rich

doi:10.1016/s0005-2728(89)80398-6

The functional catalytic unit involved in proton pumping by rat liver cytochrome-c reductase and by cytochrome-c oxidase.

AJ Moody, PR Rich

School of Biological and Marine Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

The effect of partial inhibition on the protonmotive stoichiometry of cytochrome-c reductase and cytochrome-c oxidase in intact rat liver mitochondria was examined using myxothiazol and cyanide as inhibitors, respectively. No decrease in the stoichiometry of either enzyme was found. It is shown that this result is consistent with the individual electron transfer units in each case being fully coupled to proton translocation but not with pairs of electron transfer units working in concert in dimers.

Original language	English
Pages (from-to)	29-34
Number of pages	0
Journal	Biochim Biophys Acta
Volume	973
Issue number	1
DOIs	https://doi.org/10.1016/s0005-2728(89)80398-6
Publication status	Published - 26 Jan 1989

Keywords

Animals
Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone
Cytochrome Reductases
Electron Transport
Electron Transport Complex IV
Ethylmaleimide
Ferricyanides
Kinetics
Methacrylates
Mitochondria
Liver
NADH Dehydrogenase
Oxygen Consumption
Protons
Rats
Thiazoles

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title = "The functional catalytic unit involved in proton pumping by rat liver cytochrome-c reductase and by cytochrome-c oxidase.",

abstract = "The effect of partial inhibition on the protonmotive stoichiometry of cytochrome-c reductase and cytochrome-c oxidase in intact rat liver mitochondria was examined using myxothiazol and cyanide as inhibitors, respectively. No decrease in the stoichiometry of either enzyme was found. It is shown that this result is consistent with the individual electron transfer units in each case being fully coupled to proton translocation but not with pairs of electron transfer units working in concert in dimers.",

keywords = "Animals, Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone, Cytochrome Reductases, Electron Transport, Electron Transport Complex IV, Ethylmaleimide, Ferricyanides, Kinetics, Methacrylates, Mitochondria, Liver, NADH Dehydrogenase, Oxygen Consumption, Protons, Rats, Thiazoles",

author = "AJ Moody and PR Rich",

year = "1989",

month = jan,

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doi = "10.1016/s0005-2728(89)80398-6",

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pages = "29--34",

journal = "Biochim Biophys Acta",

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T1 - The functional catalytic unit involved in proton pumping by rat liver cytochrome-c reductase and by cytochrome-c oxidase.

AU - Moody, AJ

AU - Rich, PR

PY - 1989/1/26

Y1 - 1989/1/26

N2 - The effect of partial inhibition on the protonmotive stoichiometry of cytochrome-c reductase and cytochrome-c oxidase in intact rat liver mitochondria was examined using myxothiazol and cyanide as inhibitors, respectively. No decrease in the stoichiometry of either enzyme was found. It is shown that this result is consistent with the individual electron transfer units in each case being fully coupled to proton translocation but not with pairs of electron transfer units working in concert in dimers.

AB - The effect of partial inhibition on the protonmotive stoichiometry of cytochrome-c reductase and cytochrome-c oxidase in intact rat liver mitochondria was examined using myxothiazol and cyanide as inhibitors, respectively. No decrease in the stoichiometry of either enzyme was found. It is shown that this result is consistent with the individual electron transfer units in each case being fully coupled to proton translocation but not with pairs of electron transfer units working in concert in dimers.

KW - Animals

KW - Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone

KW - Cytochrome Reductases

KW - Electron Transport

KW - Electron Transport Complex IV

KW - Ethylmaleimide

KW - Ferricyanides

KW - Kinetics

KW - Methacrylates

KW - Mitochondria

KW - Liver

KW - NADH Dehydrogenase

KW - Oxygen Consumption

KW - Protons

KW - Rats

KW - Thiazoles

U2 - 10.1016/s0005-2728(89)80398-6

DO - 10.1016/s0005-2728(89)80398-6

M3 - Article

SN - 0006-3002

VL - 973

SP - 29

EP - 34

JO - Biochim Biophys Acta

JF - Biochim Biophys Acta

IS - 1

ER -

The functional catalytic unit involved in proton pumping by rat liver cytochrome-c reductase and by cytochrome-c oxidase.

Abstract

Keywords

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