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Titolo:
Structures and proton-pumping strategies of mitochondrial respiratory enzymes
Autore:
Schultz, BE; Chan, SI;
Indirizzi:
CALTECH, Arthur Amos Noyes Lab Chem Phys, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 Noyes Lab Chem Phys, Pasadena, CA 91125 USA Acad Sinica, Inst Chem, Taipei 11529, Taiwan Acad Sinica Taipei Taiwan 11529 Sinica, Inst Chem, Taipei 11529, Taiwan
Titolo Testata:
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE
, volume: 30, anno: 2001,
pagine: 23 - 65
SICI:
1056-8700(2001)30:<23:SAPSOM>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYTOCHROME-C-OXIDASE; NADH-UBIQUINONE OXIDOREDUCTASE; BOVINE HEART-MITOCHONDRIA; ELECTRON-PARAMAGNETIC-RESONANCE; COLI FUMARATE REDUCTASE; 2 INDEPENDENT PATHWAYS; STEADY-STATE KINETICS; STRETCHING RAMAN BAND; IRON SULFUR PROTEINS; COMPLEX-I;
Keywords:
crystal structures; free energy transduction; mitochondrion; redox linkage; respiratory electron transport chain;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
147
Recensione:
Indirizzi per estratti:
Indirizzo: Chan, SI CALTECH, Arthur Amos Noyes Lab Chem Phys, Pasadena, CA 91125 USA CALTECH Pasadena CA USA 91125 Chem Phys, Pasadena, CA 91125 USA
Citazione:
B.E. Schultz e S.I. Chan, "Structures and proton-pumping strategies of mitochondrial respiratory enzymes", ANN R BIO B, 30, 2001, pp. 23-65

Abstract

Enzymes of the mitochondrial respiratory chain serve as proton pumps, using the energy made available from electron transfer reactions to transport protons across the inner mitochondrial membrane and create an electrochemical gradient used for the production of ATP. The ATP synthase enzyme is reversible and can also serve as a proton pump by coupling ATP hydrolysis to proton translocation. Each of the respiratory enzymes uses a different strategy for performing proton pumping. In this work, the strategies are describedand the structural bases for the action of these proteins are discussed inlight of recent crystal structures of several respiratory enzymes. The mechanisms and efficiency of proton translocation are also analyzed in terms of the thermodynamics of the substrate transformations catalyzed by these enzymes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 07:23:17