Kinetic study of the reduction of water to hydrogen by reduced methyl viologen mediated by platinised alumina

Andrew Mills; Peter Douglas; Tom Russell

doi:10.1039/ft9908601417

Kinetic study of the reduction of water to hydrogen by reduced methyl viologen mediated by platinised alumina

Journal of the Chemical Society Faraday Transactions ◽

10.1039/ft9908601417 ◽

1990 ◽

Vol 86 (9) ◽

pp. 1417 ◽

Cited By ~ 5

Author(s):

Andrew Mills ◽

Peter Douglas ◽

Tom Russell

Keyword(s):

Kinetic Study ◽

Methyl Viologen

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Kinetic study of the formation of oxo diperoxo complexes of molybdenum(VI) and tungsten(VI) and their reduction by iron(II), europium(II), the methyl viologen radical cation, and the dithionite ion

Inorganic Chemistry ◽

10.1021/ic00320a003 ◽

1989 ◽

Vol 28 (21) ◽

pp. 3938-3946 ◽

Cited By ~ 8

Author(s):

Lisa M. Schwane ◽

Richard C. Thompson

Keyword(s):

Kinetic Study ◽

Radical Cation ◽

Methyl Viologen ◽

Dithionite Ion ◽

And Tungsten

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Kinetic study of the photo-induced electron transfer reaction between ruthenium(ii) complexes of 2,2′-bipyridine derivatives and methyl viologen. Effects of bulky substituents introduced onto 2,2′-bipyridine

Dalton Transactions ◽

10.1039/b207048k ◽

2003 ◽

pp. 692-698 ◽

Cited By ~ 8

Author(s):

Taisuke Hamada ◽

Sei-ichi Tanaka ◽

Hiroaki Koga ◽

Yumi Sakai ◽

Shigeyoshi Sakaki

Keyword(s):

Electron Transfer ◽

Kinetic Study ◽

Methyl Viologen ◽

Transfer Reaction ◽

Electron Transfer Reaction ◽

Photo Induced Electron Transfer

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A convenient electrochemical preparation of reduced methyl viologen and a kinetic study of the reaction with oxygen using an anaerobic stopped-flow apparatus

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/0005-2728(74)90133-9 ◽

1974 ◽

Vol 333 (3) ◽

pp. 487-496 ◽

Cited By ~ 117

Author(s):

Roger N.F. Thorneley

Keyword(s):

Kinetic Study ◽

Methyl Viologen ◽

Stopped Flow ◽

Electrochemical Preparation ◽

Flow Apparatus

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Kinetic study of the reaction of benzoyl peroxide with phenolic compounds. A technique for the evaluation of phenolic O-H bond dissociation energies

Journal de Chimie Physique ◽

10.1051/jcp/1989862057 ◽

1989 ◽

Vol 86 ◽

pp. 2057-2066 ◽

Cited By ~ 2

Author(s):

Claire Rousseau-Richard ◽

Claude Richard ◽

René Martin

Keyword(s):

Phenolic Compounds ◽

Kinetic Study ◽

Benzoyl Peroxide ◽

Bond Dissociation Energies ◽

Bond Dissociation ◽

Dissociation Energies

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A kinetic study of osmium tetroxide catalysed oxidation of methyl digol and ethyl digol by hexacyanoferrate (III) in aqueous alkaline medium

Journal de Chimie Physique ◽

10.1051/jcp/1976730283 ◽

1976 ◽

Vol 73 ◽

pp. 283-286 ◽

Cited By ~ 2

Author(s):

H. S. Singh ◽

A. K. Sisodia ◽

S. M. Singh ◽

R. K. Singh ◽

R. N. Singh

Keyword(s):

Kinetic Study ◽

Alkaline Medium ◽

Osmium Tetroxide ◽

Aqueous Alkaline Medium ◽

Catalysed Oxidation

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A kinetic study of controlling nitrogen in process for boron steel by using30N2isotope gas

Revue de Métallurgie ◽

10.1051/metal:2009004 ◽

2008 ◽

Vol 105 (12) ◽

pp. 601-608

Author(s):

Seung Min Han ◽

Dong Joon Min ◽

Joo Hyun Park ◽

Jung Ho Park ◽

Jong Min Park

Keyword(s):

Kinetic Study ◽

Boron Steel

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Kinetic Study of the Effect of Heparin on the Amidase Activity of Trypsin, Plasmin and Urokinase

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657362 ◽

1983 ◽

Vol 49 (03) ◽

pp. 199-203 ◽

Cited By ~ 10

Author(s):

V M Yomtova ◽

N A Stambolieva ◽

B M Blagoev

Keyword(s):

Kinetic Study ◽

Active Center ◽

Simultaneous Presence ◽

Amidase Activity ◽

Competitive Inhibitors ◽

Uncompetitive Inhibitor

SummaryIt was found that the effect of heparin on the amidase activity of urokinase (E C 3.4.21.31), plasmin (E C 3.4.21.7) and trypsin (E C 3.4.21.4) depended on the substrate used. No effect of heparin on the amidase activity of urokinase and trypsin was observed when Pyro Glu-Gly-Arg-p-nitroanilide (S-2444) and α-N-acetyl-L-lysine-p-nitroanilide (ALNA) were used as substrates. Heparin acted as a uncompetitive inhibitor of trypsin (Ki = 1.2×10-6 M), plasmin (Ki = 4.9×10-6 M) and urokinase (Ki = l.0×10-7 M) when Bz-Phe-Val-Arg-p-nitroanilide (S-2160), H-D-Val-Leu-Lys-p-nitroanilide (S-2251) and plasminogen, respectively, were used as substrates. These results, as well as the data obtained by studying the effect of the simultaneous presence of heparin and competitive inhibitors suggest that although heparin is not bound at the active center of these enzymes, it may influence the effectivity of catalysis.

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