Stopped-Flow Fourier Transform Infrared Spectroscopy Allows Continuous Monitoring of Azide Reduction, Carbon Monoxide Inhibition, and ATP Hydrolysis by Nitrogenase
| Autor: | Roger N. F. Thorneley, John D. Tolland |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Azides
Molybdoferredoxin Time Factors Kinetics chemistry.chemical_element Photochemistry Biochemistry Phosphates Substrate Specificity chemistry.chemical_compound Adenosine Triphosphate Non-competitive inhibition ATP hydrolysis Nitrogenase Spectroscopy Fourier Transform Infrared Magnesium Fourier transform infrared spectroscopy Carbon Monoxide Binding Sites Chemistry Hydrolysis Adenosine Monophosphate Adenosine Diphosphate Klebsiella pneumoniae Models Chemical Azide Oxidation-Reduction Protein Binding Carbon monoxide |
| Zdroj: | Biochemistry. 44:9520-9527 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi050453m |
| Popis: | Stopped-flow FTIR spectroscopy was used to monitor continuously the pre-steady- and steady-state phases of azide reduction by nitrogenase and the accompanying hydrolysis of ATP. This was characterized by a ca. 1.3 s lag phase that is explained by the number of Fe protein cycles required to effect the reductions of azide to N(2) + NH(3), N(2)H(4) + NH(3), or 3NH(3). Extrapolation of the steady-state time course for azide reduction to zero time showed that one azide binds within 200 ms to each FeMo cofactor. Inhibition of azide reduction by CO was established at times |
| Databáze: | OpenAIRE |
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