Benjaminas Valiauga, N. Rouhier, J. Jacquot, N. Čėnas
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引用次数: 1
Abstract
2 Université de Lorraine, INRAE, IAM, F-54500 Vandoeuvre-les-Nancy, France The fluorescence properties of FAD of Thermotoga maritima thioredoxin reductase (TmTR), taken together with the amino acid sequences and structures of similar TRs, are consistent with the interdomain rotation in the catalysis of TmTR. The standard redox potential of FAD of TmTR, –0.230 V, determined by the reactions with 3-acetylpyridine adenine dinucleotide (APAD+/APADH) redox couple, is close to that of E. coli TR. During the reduction of duroquinone with TmTR, the transient formation of neutral FAD semiquinone, and, possibly, FADH2–NAD + complex was observed. This shows that in spite of obligatory twoelectron (hydride)-transfer between NADH and physiological disulfide oxidants, the FAD cofactor of TmTR may exist under a stable semiquinone form.
2洛林大学，INRAE，IAM，F-54500 Vandoeuvre les Nancy，France海洋热托加硫氧还蛋白还原酶（TmTR）的FAD的荧光性质，连同类似TR的氨基酸序列和结构，与TmTR催化中的结构域间旋转一致。通过与3-乙酰吡啶腺嘌呤二核苷酸（APAD+/APADH）氧化还原对的反应确定的TmTR的FAD的标准氧化还原电位为–0.230 V，与大肠杆菌TR的氧化还原电位接近。在用TmTR还原杜洛醌的过程中，观察到中性FAD半醌的瞬时形成，可能还有FADH2–NAD+复合物。这表明，尽管NADH和生理性二硫化物氧化剂之间存在强制性的二电子（氢化物）转移，但TmTR的FAD辅因子可能以稳定的半醌形式存在。
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