Functional Analogues of Cytochrome c Oxidase, Myoglobin, and Hemoglobin

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

612 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 languageEnglish
Pages (from-to)561-588
Number of pages28
JournalChemical Reviews
Volume104
Issue number2
DOIs
Publication statusPublished - Feb 2004
Externally publishedYes

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