Correction for creatine interference with the direct indophenol measurement of NH3 in steady-state nitrogenase assays

M.J. Dilworth; M.E. Eldridge; R.R. Eady

doi:10.1016/0003-2697(92)90491-O

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Correction for creatine interference with the direct indophenol measurement of NH3 in steady-state nitrogenase assays

Journal article

Peer reviewed

Correction for creatine interference with the direct indophenol measurement of NH3 in steady-state nitrogenase assays

M.J. Dilworth, M.E. Eldridge and R.R. Eady

Analytical Biochemistry, Vol.207(1), pp.6-10

1992

DOI: https://doi.org/10.1016/0003-2697(92)90491-O

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Abstract

Creatine was identified as a major source of interference with the direct phenol/hypochlorite colorimetric determination of ammonia in nitrogenase reaction mixtures. A method is described for removing other compounds which inhibit color development and for compensating for the interference produced by creatine. This method avoids time-consuming microdiffusion and also routinely makes available the efficiency of ATP hydrolysis coupled to substrate reduction (View the MathML source ratio) with N2 as a reducible substrate. Using this method we determined values for this ratio at 30°C of 4.87 ± 0.03 during the reduction of protons to H2 and 7.16 ± 0.14 during the reduction of N2 by the vanadium-containing nitrogenase of Azotobacter chroococcum.

Details

Title: Correction for creatine interference with the direct indophenol measurement of NH3 in steady-state nitrogenase assays
Authors/Creators: M.J. Dilworth (Author/Creator) - Murdoch University
M.E. Eldridge (Author/Creator) - University of Sussex
R.R. Eady (Author/Creator) - University of Sussex
Publication Details: Analytical Biochemistry, Vol.207(1), pp.6-10
Publisher: Academic Press
Identifiers: 991005541301107891
Copyright: © 1992 Published by Elsevier Inc.
Murdoch Affiliation: School of Biological and Environmental Sciences
Language: English
Resource Type: Journal article

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Collaboration types: Domestic collaboration; International collaboration
Citation topics: 2 Chemistry; 2.276 Metalloenzymes; 2.276.654 Metalloenzyme Models
Web Of Science research areas: Biochemical Research Methods; Biochemistry & Molecular Biology; Chemistry, Analytical
ESI research areas: Biology & Biochemistry