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Structural relaxation and nonexponential kinetics of CO-binding to horse myoglobin. Multiple flash photolysis experiments.

The geminate recombination kinetics of CO-myoglobin strongly deviates from single exponential behavior in contrast to what is expected for unimolecular reactions (1). At low temperatures, this result was attributed to slowly exchanging conformational states which differ substantially in barrier heig...

詳細記述

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書誌詳細
主要な著者: Post, F, Doster, W, Karvounis, G, Settles, M
フォーマット: Artigo
言語:Inglês
出版事項: 1993
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC1262517/
https://ncbi.nlm.nih.gov/pubmed/8369410
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