An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation

Claudia Binda; Reeder M. Robinson; Julia S. Martin Del Campo; Nicholas D. Keul; Pedro J. Rodriguez; Howard H. Robinson; Andrea Mattevi; Pablo Sobrado

doi:10.1074/jbc.M114.629485

An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation

Claudia Binda
, Reeder M. Robinson
, Julia S. Martin Del Campo
, Nicholas D. Keul
, Pedro J. Rodriguez
, Howard H. Robinson
, Andrea Mattevi
, Pablo Sobrado

University of Pavia
Virginia Polytechnic Institute and State University
Brookhaven National Laboratory

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

Original language	English
Pages (from-to)	12676-12688
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	290
Issue number	20
DOIs	https://doi.org/10.1074/jbc.M114.629485
State	Published - May 15 2015
Externally published	Yes

ASJC Scopus Subject Areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M114.629485

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Binda, C., Robinson, R. M., Martin Del Campo, J. S., Keul, N. D., Rodriguez, P. J., Robinson, H. H., Mattevi, A., & Sobrado, P. (2015). An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation. Journal of Biological Chemistry, 290(20), 12676-12688. https://doi.org/10.1074/jbc.M114.629485

An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation. / Binda, Claudia; Robinson, Reeder M.; Martin Del Campo, Julia S. et al.
In: Journal of Biological Chemistry, Vol. 290, No. 20, 15.05.2015, p. 12676-12688.

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

Binda, C, Robinson, RM, Martin Del Campo, JS, Keul, ND, Rodriguez, PJ, Robinson, HH, Mattevi, A & Sobrado, P 2015, 'An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation', Journal of Biological Chemistry, vol. 290, no. 20, pp. 12676-12688. https://doi.org/10.1074/jbc.M114.629485

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author = "Claudia Binda and Robinson, \{Reeder M.\} and \{Martin Del Campo\}, \{Julia S.\} and Keul, \{Nicholas D.\} and Rodriguez, \{Pedro J.\} and Robinson, \{Howard H.\} and Andrea Mattevi and Pablo Sobrado",

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AU - Binda, Claudia

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AU - Martin Del Campo, Julia S.

AU - Keul, Nicholas D.

AU - Rodriguez, Pedro J.

AU - Robinson, Howard H.

AU - Mattevi, Andrea

AU - Sobrado, Pablo

PY - 2015/5/15

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JO - Journal of Biological Chemistry

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IS - 20

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An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation

ASJC Scopus Subject Areas

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