Peck H D, LeGall J
Philos Trans R Soc Lond B Biol Sci. 1982 Sep 13;298(1093):443-66. doi: 10.1098/rstb.1982.0091.
Extensive information is available on the enzymology of respiratory sulphate reduction and the structure of electron transfer proteins isolated from the sulphate-reducing bacteria; however, it has not yet been possible to delineate satisfactorily the function of these electron transfer proteins in terms of the enzymes involved in respiratory sulphate reduction. New information about differences in pyrophosphate metabolism by Desulfovibrio and Desulfotomaculum, cellular localizations of electron transfer proteins and enzymes, and the concepts of vectorial electron transfer plus hydrogen cycling suggest that previous data on the function of electron transfer proteins must be re-evaluated and new experimental approaches designed before the problem is resolved. New information on the enzymology of lactate dehydrogenase, pyruvate dehydrogenase, adenylyl sulphate reductase, bisulphite reductase and hydrogenase is presented and discussed in the context of enzyme localization and specifically for electron transfer proteins. The function of cytochrome c3 (Mr = 13000) in the mechanism of the periplasmic hydrogenase and the role of the new [3Fe-3S] non-haem iron centres in electron transfer is emphasized.
关于呼吸性硫酸盐还原的酶学以及从硫酸盐还原细菌中分离出的电子传递蛋白的结构，已有大量信息；然而，就参与呼吸性硫酸盐还原的酶而言，尚未能够令人满意地描述这些电子传递蛋白的功能。关于脱硫弧菌和脱硫肠状菌焦磷酸代谢的差异、电子传递蛋白和酶的细胞定位以及向量电子传递加氢循环的概念的新信息表明，在解决该问题之前，必须重新评估关于电子传递蛋白功能的先前数据，并设计新的实验方法。本文在酶定位的背景下，特别是针对电子传递蛋白，介绍并讨论了乳酸脱氢酶、丙酮酸脱氢酶、腺苷硫酸还原酶、亚硫酸氢盐还原酶和氢化酶的酶学新信息。强调了细胞色素c3（Mr = 13000）在周质氢化酶机制中的功能以及新的[3Fe-3S]非血红素铁中心在电子传递中的作用。
