The pH dependence of intramolecular electron transfer rates in sulfite oxidase at high and low anion concentrations

1999 ◽  
Vol 4 (4) ◽  
pp. 390-401 ◽  
Author(s):  
Andrew Pacheco ◽  
James T. Hazzard ◽  
G. Tollin ◽  
J. H. Enemark
Keyword(s):  
Electron Transfer ◽  
Ph Dependence ◽  
Sulfite Oxidase ◽  
Intramolecular Electron Transfer ◽  
Transfer Rates

Intramolecular electron transfer controls nitrite reduction in molybdenum-containing sulfite oxidase

Nitric Oxide ◽  
2014 ◽  
Vol 42 ◽  
pp. 113
Author(s):  
Guenter Schwarz ◽  
Sabina Krizowski ◽  
Jun Wang ◽  
Dimitri Niks ◽  
Courtney Sparacino-Watkins ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Sulfite Oxidase ◽  
Nitrite Reduction ◽  
Intramolecular Electron Transfer

Intramolecular electron-transfer rates in ferrocene-derivatized glucose oxidase

1993 ◽  
Vol 115 (16) ◽  
pp. 7053-7060 ◽  
Author(s):  
Antonella Badia ◽  
Rina Carlini ◽  
Arthur Fernandez ◽  
Fernando Battaglini ◽  
Susan R. Mikkelsen ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Glucose Oxidase ◽  
Intramolecular Electron Transfer ◽  
Transfer Rates

Mechanism of nitrite-dependent NO synthesis by human sulfite oxidase

2019 ◽  
Vol 476 (12) ◽  
pp. 1805-1815 ◽  
Author(s):  
Daniel Bender ◽  
Alexander Tobias Kaczmarek ◽  
Dimitri Niks ◽  
Russ Hille ◽  
Guenter Schwarz
Keyword(s):  
Electron Transfer ◽  
Spectroscopic Studies ◽  
Sulfite Oxidase ◽  
Nitrite Reduction ◽  
Intramolecular Electron Transfer ◽  
Intermembrane Space ◽  
Electron Transfer Mechanism ◽  
Physiological Relevance ◽  
Order Of Magnitude ◽  
Human Sulfite Oxidase

AbstractIn addition to nitric oxide (NO) synthases, molybdenum-dependent enzymes have been reported to reduce nitrite to produce NO. Here, we report the stoichiometric reduction in nitrite to NO by human sulfite oxidase (SO), a mitochondrial intermembrane space enzyme primarily involved in cysteine catabolism. Kinetic and spectroscopic studies provide evidence for direct nitrite coordination at the molybdenum center followed by an inner shell electron transfer mechanism. In the presence of the physiological electron acceptor cytochrome c, we were able to close the catalytic cycle of sulfite-dependent nitrite reduction thus leading to steady-state NO synthesis, a finding that strongly supports a physiological relevance of SO-dependent NO formation. By engineering SO variants with reduced intramolecular electron transfer rate, we were able to increase NO generation efficacy by one order of magnitude, providing a mechanistic tool to tune NO synthesis by SO.

The Pathogenic Human Sulfite Oxidase Mutants G473D and A208D Are Defective in Intramolecular Electron Transfer†

Biochemistry ◽  
2005 ◽  
Vol 44 (42) ◽  
pp. 13734-13743 ◽  
Author(s):  
Changjian Feng ◽  
Heather L. Wilson ◽  
Gordon Tollin ◽  
Andrei V. Astashkin ◽  
James T. Hazzard ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Sulfite Oxidase ◽  
Intramolecular Electron Transfer ◽  
Human Sulfite Oxidase
Sign in / Sign up

Export Citation Format

Share Document