Functional models for the oxygen binding/activating hemeproteins, myoglobin and cytochrome c oxidase

James P. Collman; Todd Eberspacher; Lei Fu; Paul C. Herrmann

doi:10.1016/S1381-1169(96)00253-1

Functional models for the oxygen binding/activating hemeproteins, myoglobin and cytochrome c oxidase

James P. Collman^*
, Todd Eberspacher
, Lei Fu
, Paul C. Herrmann

^*Corresponding author for this work

Stanford University

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

11 Citations (Scopus)

Abstract

Hemoproteins (hemoglobin and myoglobin) reversibly bind O₂ for transport and storage; other heme proteins (cytochrome c oxidase) reduce O₂ to water and couple the energy from that reaction to create a proton gradient for the eventual synthesis of ATP. This paper will describe the design and synthesis of iron porphyrins which are functional models for these oxygen binding and activating heme proteins.

Original language	English
Pages (from-to)	9-20
Number of pages	12
Journal	Journal of Molecular Catalysis A: Chemical
Volume	117
Issue number	1-3
DOIs	https://doi.org/10.1016/S1381-1169(96)00253-1
Publication status	Published - 14 Mar 1997
Externally published	Yes

Keywords

Carbon monoxide binding
Cobalt porphyrins
Copper-oxygen chemistry
Iron porphyrins
Oxygen binding

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10.1016/S1381-1169(96)00253-1

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abstract = "Hemoproteins (hemoglobin and myoglobin) reversibly bind O2 for transport and storage; other heme proteins (cytochrome c oxidase) reduce O2 to water and couple the energy from that reaction to create a proton gradient for the eventual synthesis of ATP. This paper will describe the design and synthesis of iron porphyrins which are functional models for these oxygen binding and activating heme proteins.",

keywords = "Carbon monoxide binding, Cobalt porphyrins, Copper-oxygen chemistry, Iron porphyrins, Oxygen binding",

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AU - Collman, James P.

AU - Eberspacher, Todd

AU - Fu, Lei

AU - Herrmann, Paul C.

PY - 1997/3/14

Y1 - 1997/3/14

N2 - Hemoproteins (hemoglobin and myoglobin) reversibly bind O2 for transport and storage; other heme proteins (cytochrome c oxidase) reduce O2 to water and couple the energy from that reaction to create a proton gradient for the eventual synthesis of ATP. This paper will describe the design and synthesis of iron porphyrins which are functional models for these oxygen binding and activating heme proteins.

AB - Hemoproteins (hemoglobin and myoglobin) reversibly bind O2 for transport and storage; other heme proteins (cytochrome c oxidase) reduce O2 to water and couple the energy from that reaction to create a proton gradient for the eventual synthesis of ATP. This paper will describe the design and synthesis of iron porphyrins which are functional models for these oxygen binding and activating heme proteins.

KW - Carbon monoxide binding

KW - Cobalt porphyrins

KW - Copper-oxygen chemistry

KW - Iron porphyrins

KW - Oxygen binding

UR - https://www.scopus.com/pages/publications/0030898295

U2 - 10.1016/S1381-1169(96)00253-1

DO - 10.1016/S1381-1169(96)00253-1

M3 - Article

AN - SCOPUS:0030898295

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JF - Journal of Molecular Catalysis A: Chemical

IS - 1-3

ER -

Functional models for the oxygen binding/activating hemeproteins, myoglobin and cytochrome c oxidase

Abstract

Keywords

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