源自细胞色素c的血红素肽（HP）1-50以及血红素肽：非血红素肽（NHP）非共价复合物1-50:51-104的穆斯堡尔谱：细胞色素c铁位点在水溶液中溶剂化的证据
Mössbauer spectra of the heme peptide (HP) 1-50 and the heme peptide:non-heme peptide (NHP) non-covalent complex 1-50:51-104 derived from cytochrome c: evidence for cytochrome c iron site solvation in aqueous solution.
作者信息
Adams P A, Milton R C, Silver J
机构信息
MRC Biomembrane Research Unit, University of Cape Town Medical School, Observatory, Republic of South Africa.
出版信息
Biometals. 1994 Jul;7(3):217-20. doi: 10.1007/BF00149551.
PMID:8043986
Abstract
Mössbauer spectroscopic studies on a heme peptide (HP) derived from cytochrome c and on the HP recombined non-covalently with the remaining cleaved section are reported. The results suggest that the environment of the heme site in the known crystal structure of cytochrome c may differ in detail from the environment of the heme in the working protein.
摘要
报道了对源自细胞色素c的血红素肽（HP）以及与剩余裂解片段非共价重组的HP进行的穆斯堡尔光谱研究。结果表明，细胞色素c已知晶体结构中血红素位点的环境可能与工作蛋白中血红素的环境在细节上有所不同。
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