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Russ Hille
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Articles

Mechanism of nitrite-dependent NO synthesis by human sulfite oxidase

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Daniel Bender, Alexander Tobias Kaczmarek, Dimitri Niks, Russ Hille, Guenter Schwarz
Journal: Biochemical Journal
Biochem J (2019) 476 (12): 1805–1815.
https://doi.org/10.1042/BCJ20190143
Published: 28 June 2019
View articletitled, Mechanism of nitrite-dependent NO synthesis by human sulfite oxidase
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Articles

Mesohaem substitution reveals how haem electronic properties can influence the kinetic and catalytic parameters of neuronal NO synthase

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Jesús Tejero, Ashis Biswas, Mohammad Mahfuzul Haque, Zhi-Qiang Wang, Craig Hemann, Cornelius L. Varnado, Zachary Novince, Russ Hille, Douglas C. Goodwin, Dennis J. Stuehr
Journal: Biochemical Journal
Biochem J (2011) 433 (1): 163–174.
https://doi.org/10.1042/BJ20101353
Published: 15 December 2010
View articletitled, Mesohaem substitution reveals how haem electronic properties can influence the kinetic and catalytic parameters of neuronal NO synthase
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Articles

Protein–coenzyme interactions in adenosylcobalamin-dependent glutamate mutase

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Marja S. HUHTA, Hao-Ping CHEN, Craig HEMANN, C. Russ HILLE, E. Neil G. MARSH
Journal: Biochemical Journal
Biochem J (2001) 355 (1): 131–137.
https://doi.org/10.1042/bj3550131
Published: 26 February 2001
View articletitled, Protein–coenzyme interactions in adenosylcobalamin-dependent glutamate mutase
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Articles

Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme–substrate complex

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Jaswir BASRAN, Michael J. SUTCLIFFE, Russ HILLE, Nigel S. SCRUTTON
Journal: Biochemical Journal
Biochem J (1999) 341 (2): 307–314.
https://doi.org/10.1042/bj3410307
Published: 08 July 1999
View articletitled, Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme–substrate complex
Open the PDF for Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme–substrate complex in another window