Functional Analogues of Cytochrome c Oxidase, Myoglobin, and Hemoglobin

James P. Collman; Roman Boulatov; Christopher J. Sunderland; Lei Fu

doi:10.1021/cr0206059

Functional Analogues of Cytochrome c Oxidase, Myoglobin, and Hemoglobin

James P. Collman^*, Roman Boulatov, Christopher J. Sunderland, Lei Fu

^*Corresponding author for this work

Stanford University

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

652 Citations (Scopus)

Abstract

Functional analogues of cytochrome c oxidase, myoglobin (Mb) and hemoglobin (Hb) were studied. Quantitative correlation between the properties of the O ₂-binding pocket and the O ₂ affinity of the heme were also investigated. The results show the minimum stereoelectronic requirements for reversible oxygenation of ferroheme. It was also found that embedding ferroheme in a sufficiently large hydrophobic envelope allows reversible O ₂ binding, even in protic media.

Original language	English
Pages (from-to)	561-588
Number of pages	28
Journal	Chemical Reviews
Volume	104
Issue number	2
DOIs	https://doi.org/10.1021/cr0206059
Publication status	Published - Feb 2004
Externally published	Yes

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title = "Functional Analogues of Cytochrome c Oxidase, Myoglobin, and Hemoglobin",

abstract = "Functional analogues of cytochrome c oxidase, myoglobin (Mb) and hemoglobin (Hb) were studied. Quantitative correlation between the properties of the O 2-binding pocket and the O 2 affinity of the heme were also investigated. The results show the minimum stereoelectronic requirements for reversible oxygenation of ferroheme. It was also found that embedding ferroheme in a sufficiently large hydrophobic envelope allows reversible O 2 binding, even in protic media.",

author = "Collman, \{James P.\} and Roman Boulatov and Sunderland, \{Christopher J.\} and Lei Fu",

year = "2004",

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doi = "10.1021/cr0206059",

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pages = "561--588",

journal = "Chemical Reviews",

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AU - Collman, James P.

AU - Boulatov, Roman

AU - Sunderland, Christopher J.

AU - Fu, Lei

PY - 2004/2

Y1 - 2004/2

N2 - Functional analogues of cytochrome c oxidase, myoglobin (Mb) and hemoglobin (Hb) were studied. Quantitative correlation between the properties of the O 2-binding pocket and the O 2 affinity of the heme were also investigated. The results show the minimum stereoelectronic requirements for reversible oxygenation of ferroheme. It was also found that embedding ferroheme in a sufficiently large hydrophobic envelope allows reversible O 2 binding, even in protic media.

AB - Functional analogues of cytochrome c oxidase, myoglobin (Mb) and hemoglobin (Hb) were studied. Quantitative correlation between the properties of the O 2-binding pocket and the O 2 affinity of the heme were also investigated. The results show the minimum stereoelectronic requirements for reversible oxygenation of ferroheme. It was also found that embedding ferroheme in a sufficiently large hydrophobic envelope allows reversible O 2 binding, even in protic media.

UR - https://www.scopus.com/pages/publications/1542334754

U2 - 10.1021/cr0206059

DO - 10.1021/cr0206059

M3 - Article

C2 - 14871135

AN - SCOPUS:1542334754

SN - 0009-2665

VL - 104

SP - 561

EP - 588

JO - Chemical Reviews

JF - Chemical Reviews

IS - 2

ER -

Functional Analogues of Cytochrome c Oxidase, Myoglobin, and Hemoglobin

Abstract

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