Hydrogen Production by the Naked Active Site of the Di-iron Hydrogenases in Water

2009 ◽  
Vol 113 (39) ◽  
pp. 13096-13106 ◽  
Author(s):  
Federico Zipoli ◽  
Roberto Car ◽  
Morrel H. Cohen ◽  
Annabella Selloni
ChemCatChem ◽  
2017 ◽  
Vol 9 (22) ◽  
pp. 4268-4274 ◽  
Author(s):  
Zhi Jiang ◽  
Mark A. Isaacs ◽  
Zheng Wen Huang ◽  
Wenfeng Shangguan ◽  
Yifeng Deng ◽  
...  

2012 ◽  
Vol 48 (79) ◽  
pp. 9816 ◽  
Author(s):  
Anindya Roy ◽  
Christopher Madden ◽  
Giovanna Ghirlanda

2014 ◽  
Vol 47 (8) ◽  
pp. 2621-2630 ◽  
Author(s):  
Bojana Ginovska-Pangovska ◽  
Arnab Dutta ◽  
Matthew L. Reback ◽  
John C. Linehan ◽  
Wendy J. Shaw

2014 ◽  
Vol 33 (20) ◽  
pp. 5897-5906 ◽  
Author(s):  
James C. Lansing ◽  
James M. Camara ◽  
Danielle E. Gray ◽  
Thomas B. Rauchfuss

2012 ◽  
Vol 393 (10) ◽  
pp. 1089-1100 ◽  
Author(s):  
Satoshi Watanabe ◽  
Daisuke Sasaki ◽  
Taiga Tominaga ◽  
Kunio Miki

Abstract [NiFe] hydrogenases catalyze reversible hydrogen production/consumption. The active site of [NiFe] hydrogenases contains a complex NiFe(CN)2CO center, and the biosynthesis/maturation of these enzymes is a complex and dynamic process, primarily involving six Hyp proteins (HypABCDEF). HypA and HypB are involved in the Ni insertion, whereas the other four Hyp proteins (HypCDEF) are required for the biosynthesis, assembly and insertion of the Fe(CN)2CO group. Over the last decades, a large number of functional and structural studies on maturation proteins have been performed, revealing detailed functions of each Hyp protein and the framework of the maturation pathway. This article will focus on recent advances in structural studies of the Hyp proteins and on mechanistic insights into the [NiFe] hydrogenase maturation.


2016 ◽  
Vol 4 (41) ◽  
pp. 16028-16035 ◽  
Author(s):  
Huawei Huang ◽  
Chang Yu ◽  
Juan Yang ◽  
Xiaotong Han ◽  
Changtai Zhao ◽  
...  

Active site-enriched Fe2P nanodots anchored on graphene sheets (Fe2P-ND/FG) exhibit enhanced catalytic activity and stability for the hydrogen evolution reaction.


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.


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