甲酸脱氢酶
蝶呤
化学
格式化
氢化酶
辅因子
钼辅因子
脱硫弧菌
电子顺磁共振
生物化学
酶
立体化学
硫酸盐
有机化学
物理
核磁共振
催化作用
作者
Maria João Almendra,Carlos D. Brondino,Olga Yu. Gavel,Alice S. Pereira,Pedro Tavares,Sergey A. Bursakov,Duarte Araújo,Jorge Caldeira,José J. G. Moura,Isabel Moura
出处
期刊:Biochemistry
[American Chemical Society]
日期:1999-11-12
卷期号:38 (49): 16366-16372
被引量:73
摘要
An air-stable formate dehydrogenase (FDH), an enzyme that catalyzes the oxidation of formate to carbon dioxide, was purified from the sulfate reducing organism Desulfovibrio gigas (D. gigas) NCIB 9332. D. gigas FDH is a heterodimeric protein [α (92 kDa) and β (29 kDa) subunits] and contains 7 ± 1 Fe/protein and 0.9 ± 0.1 W/protein. Selenium was not detected. The UV/visible absorption spectrum of D. gigas FDH is typical of an iron−sulfur protein. Analysis of pterin nucleotides yielded a content of 1.3 ± 0.1 guanine monophosphate/mol of enzyme, which suggests a tungsten coordination with two molybdopterin guanine dinucleotide cofactors. Both Mössbauer spectroscopy performed on D. gigas FDH grown in a medium enriched with 57Fe and EPR studies performed in the native and fully reduced state of the protein confirmed the presence of two [4Fe-4S] clusters. Variable-temperature EPR studies showed the presence of two signals compatible with an atom in a d1 configuration albeit with an unusual relaxation behavior as compared to the one generally observed for W(V) ions.
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