scholarly journals Stereodynamic Quinone–Hydroquinone Molecules That Enantiomerize at sp3-Carbon via Redox-Interconversion

2017 ◽  
Vol 139 (42) ◽  
pp. 15239-15244 ◽  
Author(s):  
Byoungmoo Kim ◽  
Golo Storch ◽  
Gourab Banerjee ◽  
Brandon Q. Mercado ◽  
Janelle Castillo-Lora ◽  
...  

2018 ◽  
Vol 57 (46) ◽  
pp. 15107-15111 ◽  
Author(s):  
Golo Storch ◽  
Byoungmoo Kim ◽  
Brandon Q. Mercado ◽  
Scott J. Miller


2012 ◽  
Vol 134 (45) ◽  
pp. 18538-18541 ◽  
Author(s):  
Na Song ◽  
Christopher J. Gagliardi ◽  
Robert A. Binstead ◽  
Ming-Tian Zhang ◽  
Holden Thorp ◽  
...  


2015 ◽  
Vol 112 (37) ◽  
pp. 11455-11460 ◽  
Author(s):  
Daniel L. M. Suess ◽  
Ingmar Bürstel ◽  
Liliana De La Paz ◽  
Jon M. Kuchenreuther ◽  
Cindy C. Pham ◽  
...  

Hydrogenases catalyze the redox interconversion of protons and H2, an important reaction for a number of metabolic processes and for solar fuel production. In FeFe hydrogenases, catalysis occurs at the H cluster, a metallocofactor comprising a [4Fe–4S]H subcluster coupled to a [2Fe]H subcluster bound by CO, CN–, and azadithiolate ligands. The [2Fe]H subcluster is assembled by the maturases HydE, HydF, and HydG. HydG is a member of the radical S-adenosyl-l-methionine family of enzymes that transforms Fe and l-tyrosine into an [Fe(CO)2(CN)] synthon that is incorporated into the H cluster. Although it is thought that the site of synthon formation in HydG is the “dangler” Fe of a [5Fe] cluster, many mechanistic aspects of this chemistry remain unresolved including the full ligand set of the synthon, how the dangler Fe initially binds to HydG, and how the synthon is released at the end of the reaction. To address these questions, we herein show that l-cysteine (Cys) binds the auxiliary [4Fe–4S] cluster of HydG and further chelates the dangler Fe. We also demonstrate that a [4Fe–4S]aux[CN] species is generated during HydG catalysis, a process that entails the loss of Cys and the [Fe(CO)2(CN)] fragment; on this basis, we suggest that Cys likely completes the coordination sphere of the synthon. Thus, through spectroscopic analysis of HydG before and after the synthon is formed, we conclude that Cys serves as the ligand platform on which the synthon is built and plays a role in both Fe2+ binding and synthon release.



1997 ◽  
Vol 36 (20) ◽  
pp. 4520-4525 ◽  
Author(s):  
Colin G. Saysell ◽  
Christopher D. Borman ◽  
Andrew J. Baron ◽  
Michael J. McPherson ◽  
A. Geoffrey Sykes


2010 ◽  
Vol 363 (12) ◽  
pp. 2955-2964 ◽  
Author(s):  
K.K. Sarker ◽  
S. Saha Halder ◽  
D. Banerjee ◽  
T.K. Mondal ◽  
A.R. Paital ◽  
...  




1987 ◽  
Vol 26 (20) ◽  
pp. 3392-3398 ◽  
Author(s):  
Graeme D. Armstrong ◽  
A. Geoffrey Sykes






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