[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-571, AND CRYSTALLIZATION.
STRAIN=ACAM591;
DOI=10.1006/jsbi.1999.4139; PubMed=10479620 [NCBI, ExPASy, EBI, Israel, Japan]
Pealing S.L.,
Lysek D.A.,
Taylor P.,
Alexeev D.,
Reid G.A.,
Chapman S.K.,
Walkinshaw M.D.;
"Crystallization and preliminary X-ray analysis of flavocytochrome c(3), the fumarate reductase from Shewanella frigidimarina.";
J. Struct. Biol. 127:76-78(1999).
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[2]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1038/70045; PubMed=10581550 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor P.,
Pealing S.L.,
Reid G.A.,
Chapman S.K.,
Walkinshaw M.D.;
"Structural and mechanistic mapping of a unique fumarate reductase.";
Nat. Struct. Biol. 6:1108-1112(1999).
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[3]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-365 AND ALA-504 IN COMPLEX WITH FAD; FUMARATE AND HEMES, AND MUTAGENESIS OF HIS-365; ARG-402 AND HIS-504.
DOI=10.1021/bi000871l; PubMed=10978153 [NCBI, ExPASy, EBI, Israel, Japan]
Doherty M.K.,
Pealing S.L.,
Miles C.S.,
Moysey R.,
Taylor P.,
Walkinshaw M.D.,
Reid G.A.,
Chapman S.K.;
"Identification of the active site acid/base catalyst in a bacterial fumarate reductase: a kinetic and crystallographic study.";
Biochemistry 39:10695-10701(2000).
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[4]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-402; LYS-402 AND TYR-402, MUTAGENESIS OF ARG-402, AND ENZYME KINETICS.
DOI=10.1021/bi011360h; PubMed=11591148 [NCBI, ExPASy, EBI, Israel, Japan]
Mowat C.G.,
Moysey R.,
Miles C.S.,
Leys D.,
Doherty M.K.,
Taylor P.,
Walkinshaw M.D.,
Reid G.A.,
Chapman S.K.;
"Kinetic and crystallographic analysis of the key active site acid/base arginine in a soluble fumarate reductase.";
Biochemistry 40:12292-12298(2001).
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[5]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-505 AND TYR-505, AND CHARACTERIZATION.
DOI=10.1021/bi020155e; PubMed=12093271 [NCBI, ExPASy, EBI, Israel, Japan]
Pankhurst K.L.,
Mowat C.G.,
Miles C.S.,
Leys D.,
Walkinshaw M.D.,
Reid G.A.,
Chapman S.K.;
"Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina.";
Biochemistry 41:8551-8556(2002).
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[6]
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X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS PHE-363 AND PHE-363/ALA-402, CHARACTERIZATION, AND MASS SPECTROMETRY.
DOI=10.1021/bi0203177; PubMed=12356299 [NCBI, ExPASy, EBI, Israel, Japan]
Mowat C.G.,
Pankhurst K.L.,
Miles C.S.,
Leys D.,
Walkinshaw M.D.,
Reid G.A.,
Chapman S.K.;
"Engineering water to act as an active site acid catalyst in a soluble fumarate reductase.";
Biochemistry 41:11990-11996(2002).
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[7]
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X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ALA-61 AND MET-61 IN COMPLEXES WITH HEME; SUBSTRATE AND FAD, MASS SPECTROMETRY, AND MUTAGENESIS OF HIS-61.
DOI=10.1021/bi030159z; PubMed=14609326 [NCBI, ExPASy, EBI, Israel, Japan]
Rothery E.L.,
Mowat C.G.,
Miles C.S.,
Walkinshaw M.D.,
Reid G.A.,
Chapman S.K.;
"Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina.";
Biochemistry 42:13160-13169(2003).
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[8]
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X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANT CYS-251/CYS430.
DOI=10.1021/bi030261w; PubMed=15109257 [NCBI, ExPASy, EBI, Israel, Japan]
Rothery E.L.,
Mowat C.G.,
Miles C.S.,
Mott S.,
Walkinshaw M.D.,
Reid G.A.,
Chapman S.K.;
"Probing domain mobility in a flavocytochrome.";
Biochemistry 43:4983-4989(2004).
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[9]
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X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANTS ASP-378 AND MET-381, MASS SPECTROMETRY, AND MUTAGENESIS OF GLU-378 AND ARG-381.
DOI=10.1074/jbc.M603077200; PubMed=16699170 [NCBI, ExPASy, EBI, Israel, Japan]
Pankhurst K.L.,
Mowat C.G.,
Rothery E.L.,
Hudson J.M.,
Jones A.K.,
Miles C.S.,
Walkinshaw M.D.,
Armstrong F.A.,
Reid G.A.,
Chapman S.K.;
"A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina.";
J. Biol. Chem. 281:20589-20597(2006).
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