Crystallization And Mad Data Collection Of High-Molecular Weight Cytochrome C From Desulfovibrio Vulgaris Miyazaki F

2004 ◽  
Vol 11 (1) ◽  
pp. 93-96
Author(s):  
Naoki Shibata ◽  
Kyoko Suto ◽  
Eiko Ichimura ◽  
Kazutaka Yoshimura ◽  
Kenji Muneo ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
Data Collection ◽  
High Molecular Weight ◽  
Desulfovibrio Vulgaris

Axial coordination and reduction potentials of the 16 hemes in high-molecular-weight cytochrome c from Desulfovibrio vulgaris

1993 ◽  
Vol 51 (1-2) ◽  
pp. 28 ◽  
Author(s):  
W.R. Hagen ◽  
M.F.J.M. Verhagen ◽  
A.J. Pierik ◽  
R.B.G. Wolbert ◽  
L.F. Mallée ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
High Molecular Weight ◽  
Desulfovibrio Vulgaris ◽  
Axial Coordination ◽  
Reduction Potentials

scholarly journals A novel multi-heme structure of high molecular-weight cytochrome C fromD. vulgaris Hildenborough

2002 ◽  
Vol 58 (s1) ◽  
pp. c294-c294
Author(s):  
M. Sato ◽  
S. Nakazawa ◽  
K. Suto ◽  
N. Shibata ◽  
Y. Morimoto ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
High Molecular Weight ◽  
Heme Structure

scholarly journals Shy1p occurs in a high molecular weight complex and is required for efficient assembly of cytochrome c oxidase in yeast

FEBS Letters ◽  
2001 ◽  
Vol 498 (1) ◽  
pp. 46-51 ◽  
Author(s):  
L.G.J. Nijtmans ◽  
M. Artal Sanz ◽  
M. Bucko ◽  
M.H. Farhoud ◽  
M. Feenstra ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
High Molecular Weight ◽  
High Molecular Weight Complex

scholarly journals The High-Molecular-Weight Cytochrome c Cyc2 of Acidithiobacillus ferrooxidans Is an Outer Membrane Protein

2002 ◽  
Vol 184 (5) ◽  
pp. 1502-1502
Author(s):  
Andrés Yarzábal ◽  
Gaël Brasseur ◽  
Jeanine Ratouchniak ◽  
Karen Lund ◽  
Danielle Lemesle-Meunier ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
Membrane Protein ◽  
Outer Membrane ◽  
High Molecular Weight ◽  
Outer Membrane Protein ◽  
Acidithiobacillus Ferrooxidans

scholarly journals 2P085 Redox of high-molecular weight cytochrome c by x-ray irradiation using the microspectroscopy

2004 ◽  
Vol 44 (supplement) ◽  
pp. S131
Author(s):  
M. Sato ◽  
Y. Morimoto ◽  
N. Shibata ◽  
H. Komori ◽  
Y. Takayama ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
High Molecular Weight ◽  
X Ray

scholarly journals Five-Gene Cluster in Clostridium thermoaceticumConsisting of Two Divergent Operons Encoding Rubredoxin Oxidoreductase- Rubredoxin and Rubrerythrin–Type A Flavoprotein– High-Molecular-Weight Rubredoxin

2001 ◽  
Vol 183 (5) ◽  
pp. 1560-1567 ◽  
Author(s):  
Amaresh Das ◽  
Eric D. Coulter ◽  
Donald M. Kurtz ◽  
Lars G. Ljungdahl
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gene Cluster ◽  
Anaerobic Bacteria ◽  
Type A ◽  
Amino Acid Sequences ◽  
Desulfovibrio Vulgaris ◽  
Visible Absorption ◽  
Stress Protection ◽  
Molecular Masses

ABSTRACT A five-gene cluster encoding four nonheme iron proteins and a flavoprotein from the thermophilic anaerobic bacteriumClostridium thermoaceticum (Moorella thermoacetica) was cloned and sequenced. Based on analysis of deduced amino acid sequences, the genes were identified asrub (rubredoxin), rbo (rubredoxin oxidoreductase), rbr (rubrerythrin), fprA (type A flavoprotein), and a gene referred to as hrb(high-molecular-weight rubredoxin). Northern blot analysis demonstrated that the five-gene cluster is organized as two subclusters, consisting of two divergently transcribed operons,rbr-fprA-hrb and rbo-rub. The rbr, fprA, and rub genes were expressed inEscherichia coli, and their encoded recombinant proteins were purified. The molecular masses, UV-visible absorption spectra, and cofactor contents of the recombinant rubrerythrin, rubredoxin, and type A flavoprotein were similar to those of respective homologs from other microorganisms. Antibodies raised againstDesulfovibrio vulgaris Rbr reacted with both native and recombinant Rbr from C. thermoaceticum, indicating that this protein was expressed in the native organism. Since Rbr and Rbo have been recently implicated in oxidative stress protection in several anaerobic bacteria and archaea, we suggest a similar function of these proteins in oxygen tolerance of C. thermoaceticum.

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