Structural Insight into Poplar Glutaredoxin C1 with a Bridging Iron−Sulfur Cluster at the Active Site†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (26) ◽  
pp. 7998-8008 ◽  
Author(s):  
Yingang Feng ◽  
Nan Zhong ◽  
Nicolas Rouhier ◽  
Toshiharu Hase ◽  
Masami Kusunoki ◽  
...  
2005 ◽  
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Seigo Shima ◽  
Erica J. Lyon ◽  
Rudolf K. Thauer ◽  
Bernd Mienert ◽  
Eckhard Bill

Biochemistry ◽  
2015 ◽  
Vol 54 (2) ◽  
pp. 389-403 ◽  
Author(s):  
Katja Karstens ◽  
Stefan Wahlefeld ◽  
Marius Horch ◽  
Miriam Grunzel ◽  
Lars Lauterbach ◽  
...  

2004 ◽  
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John R. Cort ◽  
Sharon Goldsmith-Fischman ◽  
Gregory J. Kornhaber ◽  
Rong Xiao ◽  
...  

2019 ◽  
Vol 10 (1) ◽  
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Nicholas G. Fox ◽  
Xiaodi Yu ◽  
Xidong Feng ◽  
Henry J. Bailey ◽  
Alain Martelli ◽  
...  

2018 ◽  
Vol 19 (10) ◽  
pp. 3118 ◽  
Author(s):  
Marco Bortolus ◽  
Paola Costantini ◽  
Davide Doni ◽  
Donatella Carbonera

Hydrogen production in nature is performed by hydrogenases. Among them, [FeFe]-hydrogenases have a peculiar active site, named H-cluster, that is made of two parts, synthesized in different pathways. The cubane sub-cluster requires the normal iron-sulfur cluster maturation machinery. The [2Fe] sub-cluster instead requires a dedicated set of maturase proteins, HydE, HydF, and HydG that work to assemble the cluster and deliver it to the apo-hydrogenase. In particular, the delivery is performed by HydF. In this review, we will perform an overview of the latest knowledge on the maturation machinery of the H-cluster, focusing in particular on HydF.


2011 ◽  
Vol 7 (2) ◽  
pp. 306-315 ◽  
Author(s):  
Devayani P. Bhave ◽  
Jiyoung A. Hong ◽  
Rebecca L. Keller ◽  
Carsten Krebs ◽  
Kate S. Carroll

Biochemistry ◽  
2008 ◽  
Vol 47 (5) ◽  
pp. 1452-1463 ◽  
Author(s):  
Nikola Mesecke ◽  
Sarah Mittler ◽  
Elisabeth Eckers ◽  
Johannes M. Herrmann ◽  
Marcel Deponte

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