Structural Studies on Corn Nitrate Reductase: Refined Structure of the CytochromebReductase Fragment at 2.5 Å, its ADP Complex and an Active-site Mutant and …
G Lu, Y Lindqvist, G Schneider, U Dwivedi… - Journal of molecular …, 1995 - Elsevier
The refined crystal structures of the recombinant cytochromebreductase fragment of corn
(Zea mays) nitrate reductase, its ADP complex and the active-site mutant Cys242Ser are …
(Zea mays) nitrate reductase, its ADP complex and the active-site mutant Cys242Ser are …
Crystal structure of the FAD-containing fragment of corn nitrate reductase at 2.5 Å resolution: relationship to other flavoprotein reductases
G Lu, WH Campbell, G Schneider, Y Lindqvist - Structure, 1994 - cell.com
Background In the biological assimilation of nitrate in plants and microorganisms, nitrate is
reduced to ammonium by transfer of eight electrons in a two-step process. The first step of …
reduced to ammonium by transfer of eight electrons in a two-step process. The first step of …
Identification of an “essential” cysteine of nitrate reductase via mutagenesis of its recombinant cytochrome b reductase domain.
UN Dwivedi, N Shiraishi, WH Campbell - Journal of Biological Chemistry, 1994 - Elsevier
Five cysteine residues in the recombinant cytochrome b reductase domain of corn leaf
NADH: nitrate reductase (EC 1.6. 6.1) were modified by site-directed mutagenesis. At least …
NADH: nitrate reductase (EC 1.6. 6.1) were modified by site-directed mutagenesis. At least …
Spectroscopic and Kinetic Characterization of the Recombinant Wild-type and C242S Mutant of the Cytochrome b Reductase Fragment of Nitrate Reductase (∗)
K Ratnam, N Shiraishi, WH Campbell, R Hille - Journal of Biological …, 1995 - ASBMB
Spectroscopic and kinetic studies comparing the behavior of the recombinant cytochrome b
reductase fragment of corn leaf nitrate reductase and a mutant in which cysteine 242 is …
reductase fragment of corn leaf nitrate reductase and a mutant in which cysteine 242 is …
Engineering of Pyridine Nucleotide Specificity of Nitrate Reductase: Mutagenesis of Recombinant CytochromebReductase Fragment ofNeurospora crassaNADPH …
N Shiraishi, C Croy, J Kaur, WH Campbell - Archives of biochemistry and …, 1998 - Elsevier
The cytochromebreductase fragment ofNeurospora crassaNADPH: nitrate reductase (EC
1.6. 6.3) was overexpressed inEscherichia coliwith a His-tag for purification after mutation of …
1.6. 6.3) was overexpressed inEscherichia coliwith a His-tag for purification after mutation of …
Spectroscopic and Kinetic Characterization of the Recombinant Cytochrome c Reductase Fragment of Nitrate Reductase: IDENTIFICATION OF THE RATE-LIMITING …
K Ratnam, N Shiraishi, WH Campbell, R Hille - Journal of Biological …, 1997 - ASBMB
The recombinant NADH-cytochrome c reductase fragment of spinach NADH-nitrate
reductase (EC 1.6. 6.1), consisting of the contiguous heme-containing cytochrome b domain …
reductase (EC 1.6. 6.1), consisting of the contiguous heme-containing cytochrome b domain …
Nitrate reductase of Neurospora crassa: the functional role of individual amino acids in the heme domain as examined by site-directed mutagenesis
PM Okamoto, GA Marzluf - Molecular and General Genetics MGG, 1993 - Springer
The enzyme nitrate reductase, which catalyzes the reduction of nitrate to nitrite, is a multi-
redox center homodimeric protein. Each polypeptide subunit is approximately 100 kDa in …
redox center homodimeric protein. Each polypeptide subunit is approximately 100 kDa in …
High-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH: nitrate reductase and its comparison to human NADH: cytochrome …
GE Hyde, WH Campbell - Biochemical and biophysical research …, 1990 - Elsevier
Higher plant nitrate reductase can be divided into three functional domains representing its
prosthetic groups: 1) flavin; 2) cytochrome b; and 3) Mo-pterin. The flavin domain has been …
prosthetic groups: 1) flavin; 2) cytochrome b; and 3) Mo-pterin. The flavin domain has been …
[HTML][HTML] Mutational and structural analysis of the nitrate reductase heme domain of Nicotiana plumbaginifolia.
We have analyzed four Nicotiana plumbaginifolia null mutants presumably affected in the
heme domain of nitrate reductase. The DNA sequence of this domain has been determined …
heme domain of nitrate reductase. The DNA sequence of this domain has been determined …
Electrostatic properties deduced from refined structures of NADH‐cytochrome b5 reductase and the other flavin‐dependent reductases: Pyridine nucleotide‐binding …
H Nishida, K Miki - Proteins: Structure, Function, and …, 1996 - Wiley Online Library
Electrostatic properties on the protein surface were examined on the basis of the crystal
structure of NADH‐cytochrome b5 reductase refined to a crystallographic R factor of 0.223 at …
structure of NADH‐cytochrome b5 reductase refined to a crystallographic R factor of 0.223 at …
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