A functional model of cytochrome c oxidase: Thermodynamic implications

James P. Collman; Lei Fu; Paul C. Herrmann; Zhong Wang; Miroslav Rapta; Martin Bröring; Reinhold Schwenninger; Bernard Boitrel

doi:10.1002/(SICI)1521-3773(19981231)37:24<3397::AID-ANIE3397>3.0.CO;2-N

A functional model of cytochrome c oxidase: Thermodynamic implications

James P. Collman^*
, Lei Fu
, Paul C. Herrmann
, Zhong Wang
, Miroslav Rapta
, Martin Bröring
, Reinhold Schwenninger
, Bernard Boitrel

^*Corresponding author for this work

Stanford University

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

67 Citations (Scopus)

Abstract

The environment of the Cu(I) ion in the distal ligand group decides the fate of the reduction of O₂ by the two analogues 1 and 2 of the heme a₃Cu(B) center in cytochrome c oxidase. The fourfold coordination by N in 1 favors the Cu(II) oxidation state and leads to a 4e^--4H⁺ reduction and the formation of H₂O under physiological conditions, while with 2 a 2e^--2H⁺ reduction occurs to form the cytotoxic H₂O₂.

Original language	English
Pages (from-to)	3397-3400
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	37
Issue number	24
DOIs	https://doi.org/10.1002/(SICI)1521-3773(19981231)37:24<3397::AID-ANIE3397>3.0.CO;2-N
Publication status	Published - 4 Jan 1999
Externally published	Yes

Keywords

Cytochrome c oxidase
Electrochemistry
Heme proteins
N ligands
O-O activation

Access to Document

10.1002/(SICI)1521-3773(19981231)37:24<3397::AID-ANIE3397>3.0.CO;2-N

Cite this

@article{4a1b8776ba3248d185aff31adb2454ff,

title = "A functional model of cytochrome c oxidase: Thermodynamic implications",

abstract = "The environment of the Cu(I) ion in the distal ligand group decides the fate of the reduction of O2 by the two analogues 1 and 2 of the heme a3Cu(B) center in cytochrome c oxidase. The fourfold coordination by N in 1 favors the Cu(II) oxidation state and leads to a 4e--4H+ reduction and the formation of H2O under physiological conditions, while with 2 a 2e--2H+ reduction occurs to form the cytotoxic H2O2.",

keywords = "Cytochrome c oxidase, Electrochemistry, Heme proteins, N ligands, O-O activation",

author = "Collman, \{James P.\} and Lei Fu and Herrmann, \{Paul C.\} and Zhong Wang and Miroslav Rapta and Martin Br{\"o}ring and Reinhold Schwenninger and Bernard Boitrel",

year = "1999",

month = jan,

day = "4",

doi = "10.1002/(SICI)1521-3773(19981231)37:24<3397::AID-ANIE3397>3.0.CO;2-N",

language = "English",

volume = "37",

pages = "3397--3400",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "John Wiley \& Sons, Ltd",

number = "24",

}

TY - JOUR

T1 - A functional model of cytochrome c oxidase

T2 - Thermodynamic implications

AU - Collman, James P.

AU - Fu, Lei

AU - Herrmann, Paul C.

AU - Wang, Zhong

AU - Rapta, Miroslav

AU - Bröring, Martin

AU - Schwenninger, Reinhold

AU - Boitrel, Bernard

PY - 1999/1/4

Y1 - 1999/1/4

N2 - The environment of the Cu(I) ion in the distal ligand group decides the fate of the reduction of O2 by the two analogues 1 and 2 of the heme a3Cu(B) center in cytochrome c oxidase. The fourfold coordination by N in 1 favors the Cu(II) oxidation state and leads to a 4e--4H+ reduction and the formation of H2O under physiological conditions, while with 2 a 2e--2H+ reduction occurs to form the cytotoxic H2O2.

AB - The environment of the Cu(I) ion in the distal ligand group decides the fate of the reduction of O2 by the two analogues 1 and 2 of the heme a3Cu(B) center in cytochrome c oxidase. The fourfold coordination by N in 1 favors the Cu(II) oxidation state and leads to a 4e--4H+ reduction and the formation of H2O under physiological conditions, while with 2 a 2e--2H+ reduction occurs to form the cytotoxic H2O2.

KW - Cytochrome c oxidase

KW - Electrochemistry

KW - Heme proteins

KW - N ligands

KW - O-O activation

UR - https://www.scopus.com/pages/publications/0033521671

U2 - 10.1002/(SICI)1521-3773(19981231)37:24<3397::AID-ANIE3397>3.0.CO;2-N

DO - 10.1002/(SICI)1521-3773(19981231)37:24<3397::AID-ANIE3397>3.0.CO;2-N

M3 - Article

AN - SCOPUS:0033521671

SN - 1433-7851

VL - 37

SP - 3397

EP - 3400

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 24

ER -

A functional model of cytochrome c oxidase: Thermodynamic implications

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this