This page lists publications of Athel Cornish-Bowden on two enzymes involved in nitrogen metabolism in bacteria, i.e. nitrite reductase (1973-1982) and nitrate reductase (1995-present)
D1. K. J. Coleman, B. M. Newman, A. J. Cornish-Bowden & J. A. Cole (1978)
Nitrite reduction by bacteria
in
Microbiology — 1978
(ed. D. Schlessinger),
pp. 334–338, American Society of Microbiology, Washington, DC
D2. K. J. Coleman, A. Cornish-Bowden & J. A. Cole (1978)
Purification and
properties of nitrite reductase from Escherichia coli K12
Biochem. J.
175, 483–493
[Abstract]
D3. K. J. Coleman, A. Cornish-Bowden & J. A. Cole (1978)
Activation of nitrite
reductase from Escherichia coli K12 by oxidized nicotinamide–adenine dinucleotide
Biochem. J.
175, 495–499
[Abstract]
D4. R. H. Jackson, A. Cornish-Bowden & J. A. Cole (1981)
Prosthetic groups
of the NADH-dependent
nitrite reductase from Escherichia coli K12
Biochem. J.
193, 861–867
[Abstract]
D5. R. H. Jackson, J. A. Cole & A. Cornish-Bowden (1981)
The steady-state
kinetics of the NADH-dependent
nitrite reductase from Escherichia coli
K12: nitrite and hydroxylamine reduction
Biochem. J.
199, 171–178
[Abstract]
D6. R. H. Jackson, J. A. Cole & A. Cornish-Bowden (1982)
The steady-state
kinetics of the NADH-dependent
nitrite reductase from Escherichia coli
K12
Biochem. J.
203, 505–510
[Abstract]
D7. R. Cammack, R. H. Jackson, A. Cornish-Bowden & J. A. Cole (1982)
Electron
spin resonance studies of the NADH-dependent
nitrite reductase from Escherichia
coli K12
Biochem. J.
207, 333–339
[Abstract]
D8. J. Buc, C.-L. Santini, F. Blasco, R. Giordani, M. L. Cárdenas, M. Chippaux,
A. Cornish-Bowden & G. Giordano (1995)
Kinetic studies of a soluble α–β
nitrate reductase from Escherichia coli: use of various α–β mutants
with altered *gkbeta subunits
Eur. J. Biochem.
234,
766–772
[Abstract]
D9. R. Giordani, J. Buc, A. Cornish-Bowden & M. L. Cárdenas (1997)
Kinetics
of membrane-bound nitrate reductase A from Escherichia coli with analogues
of physiological electron donors: different reaction sites for menadiol and duroquinol
Eur. J. Biochem.
250, 567–577
[Abstract]