Structural interpretation of low‐temperature heme‐ligand recombination rates in myoglobin

FEBS Letters

Wildman, Timothy A.¹  Siebrand, Willem¹  Somorjai, R.L.¹ 

[1] Division of Chemistry, National Research Council of Canada, Ottawa, Ontario K1A OR6, Canada

关键词: Myoglobin;    Heme-ligand recombination;    Ligand tunneling;    Protein disorder;    Conformational substate;   

DOI  :  10.1016/0014-5793(85)80774-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The nonexponential recombination of photodissociated heme-CO and heme-O₂ in myoglobin, which is geminate at T < 180 K, is interpreted as being due to a narrow, random distribution of ligand transfer distances in the heme pocket. This permits evaluation of the most probable recombination rate which is shown to be consistent with ligand tunneling.

【 授权许可】

Unknown