scholarly journals Three-Dimensional Structure and Determinants of Stability of the Iron–Sulfur Cluster Scaffold Protein IscU from Escherichia coli

Biochemistry ◽  
2012 ◽  
Vol 51 (28) ◽  
pp. 5557-5563 ◽  
Author(s):  
Jin Hae Kim ◽  
Marco Tonelli ◽  
Taewook Kim ◽  
John L. Markley
Keyword(s):  
Escherichia Coli ◽  
Three Dimensional ◽  
Scaffold Protein ◽  
Dimensional Structure ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Three Dimensional Structure ◽  
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.

Sequence-specific1H n.m.r. assignments and determination of the three-dimensional structure of reduced escherichia coli glutaredoxin

1991 ◽  
Vol 221 (4) ◽  
pp. 1311-1324 ◽  
Author(s):  
Patrick Sodano ◽  
Tai-he Xia ◽  
John H. Bushweller ◽  
Olof Björnberg ◽  
Arne Holmgren ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

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
Sign in / Sign up

Export Citation Format

Share Document