期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 283, 期 16, 页码 10813-10821出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M710431200
关键词
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资金
- Biotechnology and Biological Sciences Research Council [BB/E002137/1, BB/E002889/1] Funding Source: researchfish
- BBSRC [BB/E002137/1, BB/E002889/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E002889/1, BB/E002137/1] Funding Source: Medline
Vitamin B-12, the antipernicious anemia factor, is the cyano derivative of adenosylcobalamin, which is one of nature's most complex coenzymes. Adenosylcobalamin is made along one of two similar yet distinct metabolic pathways, which are referred to as the aerobic and anaerobic routes. The aerobic pathway for cobalamin biosynthesis proceeds via cobalt insertion into a ring-contracted macrocycle, which is closely followed by adenosylation of the cobalt ion. An important prerequisite for adenosylation is the reduction of the centrally chelated metal from Co(II) to a highly nucleophilic Co(I) form. We have cloned a gene, cobR, encoding a biosynthetic enzyme with this co(II)rrin reductase activity from Brucella melitensis. The protein has been overproduced, and the resulting flavoprotein has been purified, characterized, and crystallized and its structure determined to 1.6 angstrom resolution. Kinetic and EPR analysis reveals that the enzyme proceeds via a semiquinone form. It is proposed that CobR may interact with the adenosyltransferase to overcome the large thermodynamic barrier required for co(II)rrin reduction.
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