Time-resolved FTIR study of CO recombination with horseradish peroxidase

Amandine Marechal; W John Ingledew; Peter R. Rich

doi:10.1042/BST0361165

Time-resolved FTIR study of CO recombination with horseradish peroxidase

Amandine Marechal, W John Ingledew, Peter R. Rich

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

Abstract

Vibrational changes associated with CO recombination to ferrous horseradish peroxidase were investigated by rapid-scan FTIR (Fourier-transform IR) spectroscopy in the 1200-2200 cm(-1) range. At pH 6.0, two conformers of bound CID are present that appear as negative bands at 1905 and 1934 cm(-1) in photolysis spectra. Their recombination rate constants are identical, confirming that they arise from two substates of bound CO that are in rapid thermal equilibrium, rather than from heterogeneous protein sites. A smaller positive band at 2134 cm(-1) also appears on photolysis and decays with the same rate constant, indicative of an intraprotein geminate site involved in recombination or, possibly, a weak-affinity surface CO-binding site. other signals arising from protein and haem in the 1700-1200 cm(-1) range can also be time-resolved with similar kinetics.

Original language	English
Pages (from-to)	1165-1168
Number of pages	4
Journal	Biochemical Society Transactions
Volume	36
DOIs	https://doi.org/10.1042/BST0361165
Publication status	Published - Dec 2008

Keywords

carbon monoxide
Fourier-transform infrared spectroscopy (FTIR spectroscopy)
horseradish peroxidase
rapid-scan
time-resolved spectroscopy
CARBON-MONOXIDE
STEP-SCAN
CATALYTIC SITE
LIGAND-BINDING
HEME POCKET
SPECTROSCOPY
MUTANTS
RESOLUTION
MYOGLOBIN
COMPLEXES

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10.1042/BST0361165

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@article{ab270ac29c2941c89a5d4ec9364becb4,

title = "Time-resolved FTIR study of CO recombination with horseradish peroxidase",

abstract = "Vibrational changes associated with CO recombination to ferrous horseradish peroxidase were investigated by rapid-scan FTIR (Fourier-transform IR) spectroscopy in the 1200-2200 cm(-1) range. At pH 6.0, two conformers of bound CID are present that appear as negative bands at 1905 and 1934 cm(-1) in photolysis spectra. Their recombination rate constants are identical, confirming that they arise from two substates of bound CO that are in rapid thermal equilibrium, rather than from heterogeneous protein sites. A smaller positive band at 2134 cm(-1) also appears on photolysis and decays with the same rate constant, indicative of an intraprotein geminate site involved in recombination or, possibly, a weak-affinity surface CO-binding site. other signals arising from protein and haem in the 1700-1200 cm(-1) range can also be time-resolved with similar kinetics.",

keywords = "carbon monoxide, Fourier-transform infrared spectroscopy (FTIR spectroscopy), horseradish peroxidase, rapid-scan, time-resolved spectroscopy, CARBON-MONOXIDE, STEP-SCAN, CATALYTIC SITE, LIGAND-BINDING, HEME POCKET, SPECTROSCOPY, MUTANTS, RESOLUTION, MYOGLOBIN, COMPLEXES",

author = "Amandine Marechal and Ingledew, {W John} and Rich, {Peter R.}",

year = "2008",

month = dec,

doi = "10.1042/BST0361165",

language = "English",

volume = "36",

pages = "1165--1168",

journal = "Biochemical Society Transactions",

issn = "0300-5127",

publisher = "Portland Press Ltd.",

}

TY - JOUR

T1 - Time-resolved FTIR study of CO recombination with horseradish peroxidase

AU - Marechal, Amandine

AU - Ingledew, W John

AU - Rich, Peter R.

PY - 2008/12

Y1 - 2008/12

N2 - Vibrational changes associated with CO recombination to ferrous horseradish peroxidase were investigated by rapid-scan FTIR (Fourier-transform IR) spectroscopy in the 1200-2200 cm(-1) range. At pH 6.0, two conformers of bound CID are present that appear as negative bands at 1905 and 1934 cm(-1) in photolysis spectra. Their recombination rate constants are identical, confirming that they arise from two substates of bound CO that are in rapid thermal equilibrium, rather than from heterogeneous protein sites. A smaller positive band at 2134 cm(-1) also appears on photolysis and decays with the same rate constant, indicative of an intraprotein geminate site involved in recombination or, possibly, a weak-affinity surface CO-binding site. other signals arising from protein and haem in the 1700-1200 cm(-1) range can also be time-resolved with similar kinetics.

AB - Vibrational changes associated with CO recombination to ferrous horseradish peroxidase were investigated by rapid-scan FTIR (Fourier-transform IR) spectroscopy in the 1200-2200 cm(-1) range. At pH 6.0, two conformers of bound CID are present that appear as negative bands at 1905 and 1934 cm(-1) in photolysis spectra. Their recombination rate constants are identical, confirming that they arise from two substates of bound CO that are in rapid thermal equilibrium, rather than from heterogeneous protein sites. A smaller positive band at 2134 cm(-1) also appears on photolysis and decays with the same rate constant, indicative of an intraprotein geminate site involved in recombination or, possibly, a weak-affinity surface CO-binding site. other signals arising from protein and haem in the 1700-1200 cm(-1) range can also be time-resolved with similar kinetics.

KW - carbon monoxide

KW - Fourier-transform infrared spectroscopy (FTIR spectroscopy)

KW - horseradish peroxidase

KW - rapid-scan

KW - time-resolved spectroscopy

KW - CARBON-MONOXIDE

KW - STEP-SCAN

KW - CATALYTIC SITE

KW - LIGAND-BINDING

KW - HEME POCKET

KW - SPECTROSCOPY

KW - MUTANTS

KW - RESOLUTION

KW - MYOGLOBIN

KW - COMPLEXES

UR - http://www.scopus.com/inward/record.url?scp=59049108330&partnerID=8YFLogxK

U2 - 10.1042/BST0361165

DO - 10.1042/BST0361165

M3 - Article

SN - 0300-5127

VL - 36

SP - 1165

EP - 1168

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

ER -

Time-resolved FTIR study of CO recombination with horseradish peroxidase

Abstract

Keywords

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