Reduction of Chemically Stable Multibonds: Nitrogenase-Like Biosynthesis of Tetrapyrroles.
Reduction of Chemically Stable Multibonds: Nitrogenase-Like Biosynthesis of Tetrapyrroles.
复制标题
化学稳定多键的还原：四吡咯的固氮酶样生物合成
DOI：
10.1007/5584_2016_175
复制
发表时间：
2017
影响因子：
--
通讯作者：
Krausze
中科院分区：
文献类型：
--
作者：
Krausze
固氮酶复杂的生物化学对四吡咯分子的生物合成起着基础性的作用，是光合作用和产甲烷的关键成分。到目前为止，已经鉴定了三种固氮酶样金属酶。叶绿素和细菌叶绿素的合成涉及原叶绿素共轭环系的C17-C18双键的还原，这是由多亚单位酶暗操作原叶绿素氧化还原酶(DPOR)催化的。随后，所有细菌-叶绿素的生物合成需要第二个类固氮酶还原C7-C8双键，称为叶绿素氧化还原酶(COR)。从机制上讲，DPOR和COR利用一种将ATP水解与构象变化联系起来的还原酶成分。这种动态的开关蛋白触发了还原酶和核心催化蛋白复合体之间的瞬时结合，从而促进了电子通过两个[4Fe4S]簇的传递。X-射线晶体结构研究结合生化实验揭示了潜在的能量传递机制的分子基础。唯一的含镍四吡咯辅助因子F430位于甲基辅酶M还原酶的活性部位，该酶催化产甲烷古菌甲烷形成的最后一步。类固氮酶蛋白NflH/Nfld被认为在F430的生物合成过程中催化一个或多个环还原步骤。目前的工作假说反映了NflH/NfLD的DPOR和COR相关的酶机制。此外，NFL编码的蛋白质被认为是位于固氮酶和DPOR/COR之间的系统发育树的基础上的“简化的”祖先。
The sophisticated biochemistry of nitrogenase plays a fundamental role for the biosynthesis of tetrapyrrole molecules, acting as key components of photosynthesis and methanogenesis. Three nitrogenase-like metalloenzymes have been characterized to date. Synthesis of chlorophylls and bacteriochlorophylls involves the reduction of the C17-C18 double bond of the conjugated ring system of protochlorophyllide which is catalyzed by the multi-subunit enzyme dark operative protochlorophyllide oxidoreductase (DPOR). Subsequently, biosynthesis of all bacteriochlorophylls requires the reduction of the C7-C8 double bond by a second nitrogenase-like enzyme termed chlorophyllide oxidoreductase (COR). Mechanistically, DPOR and COR make use of a reductase component which links ATP hydrolysis to conformational changes. This dynamic switch protein is triggering the transient association between the reductase and the core catalytic protein complex, thereby facilitating the transduction of electrons via two [4Fe4S] clusters. X-ray crystallographic structural investigations in combination with biochemical experiments revealed the molecular basis of the underlying energy transduction mechanism. The unique nickel-containing tetrapyrrole cofactor F430is located in the active site of methyl-coenzyme M reductase, which is catalyzing the final step of methane formation in methanogenic archaea. The nitrogenase-like protein NflH/NflD has been proposed to catalyze one or more ring reduction steps during the biosynthesis of F430. The present working hypothesis mirrors a DPOR and COR related enzyme mechanism of NflH/NflD. Furthermore,nfl-encoded proteins were suggested as “simplified” ancestors lying basal in the phylogenetic tree between nitrogenase and DPOR/COR.
登录
查看更多内容
影响因子：
4.8
作者：
Broecker, Markus J.;Waetzlich, Denise;Jahn, Dieter
通讯作者：
Jahn, Dieter
影响因子：
2.9
作者：
Ranjana Sarma;B. M. Barney;T. Hamilton;Alma Jones;L. Seefeldt;J. W. Peters
通讯作者：
Ranjana Sarma;B. M. Barney;T. Hamilton;Alma Jones;L. Seefeldt;J. W. Peters
镍卟啉、辅酶 F430 及其酶、甲基辅酶 M 还原酶的结构和功能。
影响因子：
11.3
作者：
H. Friedmann;A. Klein;R. Thauer
通讯作者：
R. Thauer
模拟固氮酶功能的钼催化剂固氮：DFT 和溶剂效应的批判性评估。
影响因子：
5.5
作者：
A. Magistrato;Arturo Robertazzi;P. Carloni
通讯作者：
P. Carloni
（细菌）叶绿素生物合成的嵌合类固氮酶*
DOI：
10.1074/jbc.m901331200
发表时间：
2009
期刊：
The Journal of Biological Chemistry
影响因子：
--
作者：
Wätzlich;Bröcker;Uliczka
通讯作者：
Uliczka