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Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a five- or six-coordinate Fe-NO complex. The H93G mutation eliminates the covalent attachment between the protein and ...
The resonant Raman active mode identified in numerous studies as the heme iron−histidine stretch has been systematically investigated in the Raman spectrum of 15 exogenous ligands to the heme ir...
Recently, heme protein cavity mutants have been engineered in which the proximal coordinating amino acid has been replaced by a smaller, noncoordinating residue leaving a cavity that can be filled by ...
Transient absorption spectra in the Soret region have been measured following the photolysis of human MbCO in 75%(w/w) glycerol:water at 250, 270, and 290 K. The peak of the transient difference spect...
The temperature dependences of the reduction potentials (E degrees') of wild-type human myoglobin (Mb) and three site-directed mutants have been measured by the use of thin-layer spectroelectrochemist...
专著信息 书名 An electrochemical investigation of ligand-binding abilities of film-entrapped myoglobin 语种 英文 撰写或编译 作者 Wenjun Zhang,Chunhai Fan,Yuting Sun,Genxi Li 第一作者单位 出版社 Biochimica et Biophysica Acta - ...

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