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Volumn 127, Issue 51, 2005, Pages 18179-18189

Electrochemical definitions of O2 sensitivity and oxidative inactivation in hydrogenases

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ELECTROCHEMISTRY; ENZYMES; OXIDATION; PROTEINS; REACTION KINETICS; REDOX REACTIONS; THERMODYNAMICS;

EID: 29844441433     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja055160v     Document Type: Article
Times cited : (195)

References (72)
  • 23
  • 27
    • 29844443833 scopus 로고    scopus 로고
    • note
    • This enzyme is now also considered to be membrane bound and is referred to as MBH by some authors (e.g., ref 31).
  • 57
    • 29844434675 scopus 로고    scopus 로고
    • note
    • The purification of R. eutropha [NiFe]-MBH will be published elsewhere.
  • 60
    • 29844442933 scopus 로고    scopus 로고
    • note
    • 2 is evolved at the counter electrode. We are currently designing even more rigorous experiments to address these issues.
  • 61
    • 29844436112 scopus 로고    scopus 로고
    • note
    • -2).
  • 63
    • 29844432210 scopus 로고    scopus 로고
    • note
    • However, these experiments focus on the measurement of potentials controlling catalytic activity, and the potentials do not vary between films of different coverage.
  • 65
    • 2542566229 scopus 로고    scopus 로고
    • The hydrogen-consumption activity of the [NiFe] hydrogenase of Allochromatium vinosum in different redox states
    • Cammack, R., Frey, M., Robson, R., Eds.; Taylor & Francis: London
    • Bleijlevens, B. The hydrogen-consumption activity of the [NiFe] hydrogenase of Allochromatium vinosum in different redox states. In Hydrogen as a Fuel, Learning from Nature; Cammack, R., Frey, M., Robson, R., Eds.; Taylor & Francis: London, 2001; pp 82-84.
    • (2001) Hydrogen as a Fuel, Learning from Nature , pp. 82-84
    • Bleijlevens, B.1
  • 67
    • 18744363629 scopus 로고    scopus 로고
    • In a recent study of the catalytic electron transport mechanism of E. coli fumarate reductase (Hudson, J. M.; Heffron, K.; Kotlyar, V.; Sher, Y.; Maklashina, E.; Cecchini, G.; Armstrong, F. A. J. Am. Chem. Soc. 2005, 127, 6977-6989), we showed that complex features observed in the voltammetry during electrocatalytic fumarate reduction reflected the rates and energetics of electron flow through a specific 4Fe-4S cluster in the enzyme. Voltammograms for native R. eutropha MBH (not shown) have the same appearance as that of the Strep-tagged MBH shown here, indicating that the features observed are inherent to the enzyme rather than the result of the sample history.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6977-6989
    • Hudson, J.M.1    Heffron, K.2    Kotlyar, V.3    Sher, Y.4    Maklashina, E.5    Cecchini, G.6    Armstrong, F.A.7
  • 68
    • 29844442244 scopus 로고    scopus 로고
    • note
    • 2 rather than film loss accounts for the decrease in current observed during experiments on this enzyme.
  • 69
    • 29844445957 scopus 로고    scopus 로고
    • note
    • 2.
  • 70
    • 29844438435 scopus 로고    scopus 로고
    • note
    • Kinetic measurements were carried out in triplicate, and error limits represent the standard deviation of the data set. Measurements were performed on samples of different coverage, and rates were found to be independent of coverage as expected. Here we examine the rate of change of catalytic turnover rate.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.