scholarly journals Iron-sulfur cluster carrier proteins involved in the assembly of Escherichia coli NADH:ubiquinone oxidoreductase (complex I)

2018 ◽  
Vol 111 (1) ◽  
pp. 31-45 ◽  
Author(s):  
Sabrina Burschel ◽  
Doris Kreuzer Decovic ◽  
Franziska Nuber ◽  
Marie Stiller ◽  
Maud Hofmann ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Complex I ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Carrier Proteins ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

Iron−Sulfur Cluster N7 of the NADH:Ubiquinone Oxidoreductase (Complex I) Is Essential for Stability but Not Involved in Electron Transfer†

Biochemistry ◽  
2007 ◽  
Vol 46 (22) ◽  
pp. 6588-6596 ◽  
Author(s):  
Thomas Pohl ◽  
Theresa Bauer ◽  
Katerina Dörner ◽  
Stefan Stolpe ◽  
Philipp Sell ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Complex I ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

A Possible Role for Iron-Sulfur Cluster N2 in Proton Translocation by the NADH:Ubiquinone Oxidoreductase (Complex I)

2005 ◽  
Vol 10 (2-4) ◽  
pp. 208-222 ◽  
Author(s):  
Dirk Flemming ◽  
Stefan Stolpe ◽  
Daniel Schneider ◽  
Petra Hellwig ◽  
Thorsten Friedrich
Keyword(s):  
Complex I ◽  
Proton Translocation ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

scholarly journals Functional Studies of [FeFe] Hydrogenase Maturation in an Escherichia coli Biosynthetic System

2006 ◽  
Vol 188 (6) ◽  
pp. 2163-2172 ◽  
Author(s):  
Paul W. King ◽  
Matthew C. Posewitz ◽  
Maria L. Ghirardi ◽  
Michael Seibert
Keyword(s):  
Escherichia Coli ◽  
Catalytic Domain ◽  
Expression System ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
E Coli ◽  
Functional Studies ◽  
Hydrogenase Maturation ◽  
Iron Sulfur ◽  
And Function

ABSTRACT Maturation of [FeFe] hydrogenases requires the biosynthesis and insertion of the catalytic iron-sulfur cluster, the H cluster. Two radical S-adenosylmethionine (SAM) proteins proposed to function in H cluster biosynthesis, HydEF and HydG, were recently identified in the hydEF-1 mutant of the green alga Chlamydomonas reinhardtii (M. C. Posewitz, P. W. King, S. L. Smolinski, L. Zhang, M. Seibert, and M. L. Ghirardi, J. Biol. Chem. 279:25711-25720, 2004). Previous efforts to study [FeFe] hydrogenase maturation in Escherichia coli by coexpression of C. reinhardtii HydEF and HydG and the HydA1 [FeFe] hydrogenase were hindered by instability of the hydEF and hydG expression clones. A more stable [FeFe] hydrogenase expression system has been achieved in E. coli by cloning and coexpression of hydE, hydF, and hydG from the bacterium Clostridium acetobutylicum. Coexpression of the C. acetobutylicum maturation proteins with various algal and bacterial [FeFe] hydrogenases in E. coli resulted in purified enzymes with specific activities that were similar to those of the enzymes purified from native sources. In the case of structurally complex [FeFe] hydrogenases, maturation of the catalytic sites could occur in the absence of an accessory iron-sulfur cluster domain. Initial investigations of the structure and function of the maturation proteins HydE, HydF, and HydG showed that the highly conserved radical-SAM domains of both HydE and HydG and the GTPase domain of HydF were essential for achieving biosynthesis of active [FeFe] hydrogenases. Together, these results demonstrate that the catalytic domain and a functionally complete set of Hyd maturation proteins are fundamental to achieving biosynthesis of catalytic [FeFe] hydrogenases.

Crystal Structure of IscA, an Iron-sulfur Cluster Assembly Protein from Escherichia coli

2004 ◽  
Vol 338 (1) ◽  
pp. 127-137 ◽  
Author(s):  
Jill R. Cupp-Vickery ◽  
Jonathan J. Silberg ◽  
Dennis T. Ta ◽  
Larry E. Vickery
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Cluster Assembly ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

scholarly journals A conserved lysine residue controls iron–sulfur cluster redox chemistry in Escherichia coli fumarate reductase

2013 ◽  
Vol 1827 (10) ◽  
pp. 1141-1147 ◽  
Author(s):  
Victor W.T. Cheng ◽  
Quang M. Tran ◽  
Nasim Boroumand ◽  
Richard A. Rothery ◽  
Elena Maklashina ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Redox Chemistry ◽  
Lysine Residue ◽  
Fumarate Reductase ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

scholarly journals Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthase

FEBS Letters ◽  
2000 ◽  
Vol 466 (2-3) ◽  
pp. 372-376 ◽  
Author(s):  
Kirsty S Hewitson ◽  
Jack E Baldwin ◽  
Nicholas M Shaw ◽  
Peter L Roach
Keyword(s):  
Escherichia Coli ◽  
Biotin Synthase ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur
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