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• W1995595718 endingPage "1573" @default.
• W1995595718 startingPage "1563" @default.
• W1995595718 abstract "The kinetic properties of the three taxonomic A substates of sperm whale carbonmonoxy myoglobin in 75% glycerol/buffer are studied by flash photolysis with monitoring in the infrared stretch bands of bound CO at nu(A0) approximately 1967 cm-1, nu(A1) approximately 1947 cm-1, and nu(A3) approximately 1929 cm-1 between 60 and 300 K. Below 160 K the photodissociated CO rebinds from the heme pocket, no interconversion among the A substates is observed, and rebinding in each A substate is nonexponential in time and described by a different temperature-independent distribution of enthalpy barriers with a different preexponential. Measurements in the electronic bands, e.g., the Soret, contain contributions of all three A substates and can, therefore, be only approximately modeled with a single enthalpy distribution and a single preexponential. The bond formation step at the heme is fastest for the A0 substate, intermediate for the A1 substate, and slowest for A3. Rebinding between 200 and 300 K displays several processes, including geminate rebinding, rebinding after ligand escape to the solvent, and interconversion among the A substates. Different kinetics are measured in each of the A bands for times shorter than the characteristic time of fluctuations among the A substates. At longer times, fluctuational averaging yields the same kinetics in all three A substates. The interconversion rates between A1 and A3 are determined from the time when the scaled kinetic traces of the two substates merge. Fluctuations between A1 and A3 are much faster than those between A0 and either A1 or A3, so A1 and A3 appear as one kinetic species in the exchange with A0. The maximum-entropy method is used to extract the distribution of rate coefficients for the interconversion process A0 <--> A1 + A3 from the flash photolysis data. The temperature dependencies of the A substate interconversion processes are fitted with a non-Arrhenius expression similar to that used to describe relaxation processes in glasses. At 300 K the interconversion time for A0 <--> A1 + A3 is 10 microseconds, and extrapolation yields approximately 1 ns for A1 <--> A3. The pronounced kinetic differences imply different structural rearrangements. Crystallographic data support this conclusion: They show that formation of the A0 substate involves a major change of the protein structure; the distal histidine rotates about the C(alpha)-C(beta) bond, and its imidazole sidechain swings out of the heme pocket into the solvent, whereas it remains in the heme pocket in the A1 <--> A3 interconversion. The fast A1 <--> A3 exchange is inconsistent with structural models that involve differences in the protonation between A1 and A3." @default.
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• W1995595718 date "1996-09-01" @default.
• W1995595718 modified "2023-10-16" @default.
• W1995595718 title "Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobin" @default.
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• W1995595718 cites W1507461405 @default.
• W1995595718 cites W1547838161 @default.
• W1995595718 cites W1571407241 @default.
• W1995595718 cites W1600125245 @default.
• W1995595718 cites W1849447163 @default.
• W1995595718 cites W1966211961 @default.
• W1995595718 cites W1966312962 @default.
• W1995595718 cites W1968242010 @default.
• W1995595718 cites W1970332353 @default.
• W1995595718 cites W1972014028 @default.
• W1995595718 cites W1977718959 @default.
• W1995595718 cites W1978862989 @default.
• W1995595718 cites W1980816449 @default.
• W1995595718 cites W1982063067 @default.
• W1995595718 cites W1984965754 @default.
• W1995595718 cites W1988116855 @default.
• W1995595718 cites W1997621425 @default.
• W1995595718 cites W1997676547 @default.
• W1995595718 cites W1997997381 @default.
• W1995595718 cites W1999136578 @default.
• W1995595718 cites W2000212161 @default.
• W1995595718 cites W2000569151 @default.
• W1995595718 cites W2003948232 @default.
• W1995595718 cites W2004607866 @default.
• W1995595718 cites W2007800651 @default.
• W1995595718 cites W2008407134 @default.
• W1995595718 cites W2010495215 @default.
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• W1995595718 cites W2016088806 @default.
• W1995595718 cites W2017644006 @default.
• W1995595718 cites W2017981842 @default.
• W1995595718 cites W2018265568 @default.
• W1995595718 cites W2021664957 @default.
• W1995595718 cites W2022119471 @default.
• W1995595718 cites W2026247264 @default.
• W1995595718 cites W2030568700 @default.
• W1995595718 cites W2030885149 @default.
• W1995595718 cites W2031633851 @default.
• W1995595718 cites W2038068557 @default.
• W1995595718 cites W2040355223 @default.
• W1995595718 cites W2044467649 @default.
• W1995595718 cites W2045159840 @default.
• W1995595718 cites W2057452813 @default.
• W1995595718 cites W2061066489 @default.
• W1995595718 cites W2062972508 @default.
• W1995595718 cites W2064462783 @default.
• W1995595718 cites W2070930236 @default.
• W1995595718 cites W2075333740 @default.
• W1995595718 cites W2079176793 @default.
• W1995595718 cites W2085110003 @default.
• W1995595718 cites W2085220028 @default.
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• W1995595718 cites W2109863831 @default.
• W1995595718 cites W2114615491 @default.
• W1995595718 cites W2116389268 @default.
• W1995595718 cites W2121068877 @default.
• W1995595718 cites W2132397429 @default.
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• W1995595718 doi "https://doi.org/10.1016/s0006-3495(96)79359-1" @default.
• W1995595718 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1233623" @default.
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• W1995595718 hasPublicationYear "1996" @default.
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