Redox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies.

K.L.C. Gronberg; N.J. Watmough; A.J. Thomson; D.J. Richardson; S.J. Field

doi:10.1074/jbc.M400824200

Redox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies.

K.L.C. Gronberg, N.J. Watmough, A.J. Thomson, D.J. Richardson, S.J. Field

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

Original language	English
Pages (from-to)	17120-17125
Number of pages	6
Journal	Journal of Biological Chemistry
Volume	279
Issue number	17
DOIs	https://doi.org/10.1074/jbc.M400824200
Publication status	Published - 2004

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10.1074/jbc.M400824200

http://dx.doi.org/10.1074/jbc.M400824200

Cite this

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title = "Redox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies.",

author = "K.L.C. Gronberg and N.J. Watmough and A.J. Thomson and D.J. Richardson and S.J. Field",

year = "2004",

doi = "10.1074/jbc.M400824200",

language = "English",

volume = "279",

pages = "17120--17125",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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Redox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies. / Gronberg, K.L.C.; Watmough, N.J.; Thomson, A.J.; Richardson, D.J.; Field, S.J.

In: Journal of Biological Chemistry, Vol. 279, No. 17, 2004, p. 17120-17125.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Redox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies.

AU - Gronberg, K.L.C.

AU - Watmough, N.J.

AU - Thomson, A.J.

AU - Richardson, D.J.

AU - Field, S.J.

PY - 2004

Y1 - 2004

U2 - 10.1074/jbc.M400824200

DO - 10.1074/jbc.M400824200

M3 - Article

VL - 279

SP - 17120

EP - 17125

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 17

ER -