Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides.
Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides.
复制标题
细胞色素氧化酶中高自旋血红素轴向配体的身份:大肠杆菌 bo 型氧化酶和球形红杆菌 aa3 型氧化酶突变体的光谱表征。
DOI:
10.1021/bi00091a046
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发表时间:
1993
期刊:
影响因子:
2.9
通讯作者:
Gennis,RB
中科院分区:
文献类型:
--
作者:
Calhoun,MW;Thomas,JW;Hill,JJ;Hosler,JP;Shapleigh,JP;Tecklenburg,MM;Ferguson-Miller,S;Babcock,GT;Alben,JO;Gennis,RB
MATERIALS AND METHODSMaterials. Restriction endonucleases and DNA modifying enzymes were obtained from New England Biolabs, Bethesda Research Laboratories, or United States Biochemical Corp. Oligonucleotides used in the generation of mutants and for DNA sequencing were obtained from the Biotechnology Center at the University of Illinois at Urbana-Champaign.