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 …

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 …

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 …

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 …

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 …

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 …

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 …

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 …

[HTML][HTML] Mutational and structural analysis of the nitrate reductase heme domain of Nicotiana plumbaginifolia.

C Meyer, JM Levin, JM Roussel, P Rouze - Journal of Biological Chemistry, 1991 - Elsevier
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 …

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 …