Insights into the Mechanism ofPseudomonas dacunhaeAspartate β-Decarboxylase from Rapid-Scanning Stopped-Flow Kinetics

Robert S. Phillips; Santiago Lima; Roman Khristoforov; Bakthavatsalam Sudararaju

doi:10.1021/bi100272g

Insights into the Mechanism ofPseudomonas dacunhaeAspartate β-Decarboxylase from Rapid-Scanning Stopped-Flow Kinetics

Biochemistry ◽

10.1021/bi100272g ◽

2010 ◽

Vol 49 (24) ◽

pp. 5066-5073 ◽

Cited By ~ 7

Author(s):

Robert S. Phillips ◽

Santiago Lima ◽

Roman Khristoforov ◽

Bakthavatsalam Sudararaju

Keyword(s):

Stopped Flow ◽

Stopped Flow Kinetics ◽

Rapid Scanning

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Principal component analysis of rapid scanning wavelength stopped-flow kinetics experiments on the liver alcohol dehydrogenase catalyzed reduction of p-nitroso-N,N-dimethylaniline by 1,4-dihydronicotinamide adenine dinucleotide

The Journal of Physical Chemistry ◽

10.1021/j100457a017 ◽

1980 ◽

Vol 84 (20) ◽

pp. 2567-2575 ◽

Cited By ~ 8

Author(s):

R. N. Cochran ◽

F. H. Horne ◽

J. L. Dye ◽

J. Ceraso ◽

C. H. Suelter

Keyword(s):

Principal Component Analysis ◽

Alcohol Dehydrogenase ◽

Principal Component ◽

Component Analysis ◽

Stopped Flow ◽

Liver Alcohol Dehydrogenase ◽

Stopped Flow Kinetics ◽

Rapid Scanning

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Stopped flow kinetics of carbamylcholine binding to membrane bound acetylcholine receptor

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(78)91444-4 ◽

1978 ◽

Vol 81 (3) ◽

pp. 955-964 ◽

Cited By ~ 22

Author(s):

U. Quast ◽

M. Schimerlik ◽

M.A. Raftery

Keyword(s):

Acetylcholine Receptor ◽

Stopped Flow ◽

Membrane Bound ◽

Stopped Flow Kinetics ◽

Kinetics Of

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Stopped-Flow Ultra-Rapid-Scanning Fourier Transform Infrared Spectroscopy on the Millisecond Time Scale

Applied Spectroscopy ◽

10.1366/000370210792081019 ◽

2010 ◽

Vol 64 (8) ◽

pp. 907-911 ◽

Cited By ~ 3

Author(s):

Matthew L. Reback ◽

Christopher W. Roske ◽

Thomas E. Bitterwolf ◽

Peter R. Griffiths ◽

Christopher J. Manning

Keyword(s):

Fourier Transform ◽

Infrared Spectroscopy ◽

Fourier Transform Infrared Spectroscopy ◽

Time Scale ◽

Fourier Transform Infrared ◽

Stopped Flow ◽

Millisecond Time Scale ◽

Rapid Scanning

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Variable temperature computerized dual-beam, rapid scanning stopped-flow apparatus for the study of air-sensitive systems and transients in enzyme reactions

Analytical Chemistry ◽

10.1021/ac60359a004 ◽

1975 ◽

Vol 47 (9) ◽

pp. 1644-1649 ◽

Cited By ~ 25

Author(s):

Nicholas. Papadakis ◽

Richard B. Coolen ◽

James L. Dye

Keyword(s):

Variable Temperature ◽

Stopped Flow ◽

Enzyme Reactions ◽

Dual Beam ◽

Flow Apparatus ◽

Rapid Scanning

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Stopped-Flow Kinetics Investigation of the Imidazole-Catalyzed Peroxyoxalate Chemiluminescence Reaction

The Journal of Organic Chemistry ◽

10.1021/jo9722109 ◽

1998 ◽

Vol 63 (9) ◽

pp. 3023-3031 ◽

Cited By ~ 32

Author(s):

Andrew G. Hadd ◽

Alex L. Robinson ◽

Kathy L. Rowlen ◽

John W. Birks

Keyword(s):

Stopped Flow ◽

Peroxyoxalate Chemiluminescence ◽

Stopped Flow Kinetics

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Conformational gating of the dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Synthesis, characterization, and stopped-flow kinetics studies of 1,5-IAEDANS-labeled desulfoviridin

Biochemistry ◽

10.1021/bi00203a017 ◽

1994 ◽

Vol 33 (37) ◽

pp. 11209-11216 ◽

Cited By ~ 8

Author(s):

Siu Man Lui ◽

J. A. Cowan

Keyword(s):

Sulfite Reductase ◽

Desulfovibrio Vulgaris ◽

Stopped Flow ◽

Kinetics Studies ◽

Dissimilatory Sulfite Reductase ◽

Desulfovibrio Vulgaris Hildenborough ◽

Stopped Flow Kinetics ◽

Conformational Gating

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Characterization of the functional role of a flexible loop in the .alpha.-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesis

Biochemistry ◽

10.1021/bi00090a016 ◽

1993 ◽

Vol 32 (39) ◽

pp. 10404-10413 ◽

Cited By ~ 40

Author(s):

Peter S. Brzovic ◽

C. Craig Hyde ◽

Edith W. Miles ◽

Michael F. Dunn

Keyword(s):

Functional Role ◽

Site Directed Mutagenesis ◽

Alpha Subunit ◽

Directed Mutagenesis ◽

Stopped Flow ◽

Tryptophan Synthase ◽

Flexible Loop ◽

Rapid Scanning

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Rapid scanning stopped-flow absorption studies of the effect on tryptophanase of a change in pH or potassium(1+) ion concentration: evidence for a slow conformational change

Journal of the American Chemical Society ◽

10.1021/ja00502a056 ◽

1979 ◽

Vol 101 (8) ◽

pp. 2218-2219 ◽

Cited By ~ 9

Author(s):

David S. June ◽

Barbara Kennedy ◽

T. H. Pierce ◽

Sami V. Elias ◽

Folim Halaka ◽

...

Keyword(s):

Conformational Change ◽

Ion Concentration ◽

Stopped Flow ◽

Absorption Studies ◽

Rapid Scanning

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Stopped-flow kinetics and cysteine residue protonation of human isobutyryl-CoA dehydrogenase

Egyptian Journal of Pure and Applied Science ◽

10.21608/ejaps.2017.183755 ◽

2017 ◽

Vol 55 (1) ◽

pp. 41-47

Keyword(s):

Cysteine Residue ◽

Stopped Flow ◽

Stopped Flow Kinetics

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Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies

Biochemical Journal ◽

10.1042/bj2430079 ◽

1987 ◽

Vol 243 (1) ◽

pp. 79-86 ◽

Cited By ~ 4

Author(s):

S R Patanjali ◽

M J Swamy ◽

A Surolia

Keyword(s):

Amino Acid ◽

Protein A ◽

Stopped Flow ◽

Amino Acid Residues ◽

Acidic Amino Acid ◽

Native Protein ◽

Tryptophan Residues ◽

Stopped Flow Kinetics ◽

Two Phases ◽

Kinetics Of

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.

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