Dynamics of carbon monoxide binding by heme proteins

R. H. Austin; K. Beeson; L. Eisenstein; H. Frauenfelder; I. C. Gunsalus; V. P. Marshall

doi:10.1126/science.181.4099.541

Dynamics of carbon monoxide binding by heme proteins

R. H. Austin
, K. Beeson
, L. Eisenstein
, H. Frauenfelder
, I. C. Gunsalus
, V. P. Marshall

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

59 Scopus citations

Abstract

Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50°K for myoglobin and 25°K for cytochrome P-450 in glycerol-water solution. Above 240°K the reaction is second order; between 240° and 200°K the rebinding becomes exponential and independent of the carbon monoxide concentration. Below 150°K the reaction follows a power law and is approximately 10³ times faster for cytochrome P-450 than for myoglobin.

Original language	English (US)
Pages (from-to)	541-543
Number of pages	3
Journal	Science
Volume	181
Issue number	4099
DOIs	https://doi.org/10.1126/science.181.4099.541
State	Published - 1973
Externally published	Yes

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title = "Dynamics of carbon monoxide binding by heme proteins",

abstract = "Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50°K for myoglobin and 25°K for cytochrome P-450 in glycerol-water solution. Above 240°K the reaction is second order; between 240° and 200°K the rebinding becomes exponential and independent of the carbon monoxide concentration. Below 150°K the reaction follows a power law and is approximately 103 times faster for cytochrome P-450 than for myoglobin.",

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year = "1973",

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T1 - Dynamics of carbon monoxide binding by heme proteins

AU - Austin, R. H.

AU - Beeson, K.

AU - Eisenstein, L.

AU - Frauenfelder, H.

AU - Gunsalus, I. C.

AU - Marshall, V. P.

PY - 1973

Y1 - 1973

N2 - Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50°K for myoglobin and 25°K for cytochrome P-450 in glycerol-water solution. Above 240°K the reaction is second order; between 240° and 200°K the rebinding becomes exponential and independent of the carbon monoxide concentration. Below 150°K the reaction follows a power law and is approximately 103 times faster for cytochrome P-450 than for myoglobin.

AB - Rebinding of carbon monoxide to myoglobin and to cytochrome P-450 after removal by a light flash occurs down to 50°K for myoglobin and 25°K for cytochrome P-450 in glycerol-water solution. Above 240°K the reaction is second order; between 240° and 200°K the rebinding becomes exponential and independent of the carbon monoxide concentration. Below 150°K the reaction follows a power law and is approximately 103 times faster for cytochrome P-450 than for myoglobin.

UR - https://www.scopus.com/pages/publications/0015882273

UR - https://www.scopus.com/pages/publications/0015882273#tab=citedBy

U2 - 10.1126/science.181.4099.541

DO - 10.1126/science.181.4099.541

M3 - Article

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AN - SCOPUS:0015882273

SN - 0036-8075

VL - 181

SP - 541

EP - 543

JO - Science

JF - Science

IS - 4099

ER -

Dynamics of carbon monoxide binding by heme proteins

Abstract

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