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Deng, Hua, Burgner, John, Callender, Robert (1992) Raman spectroscopic studies of the effects of substrate binding on coenzymes bound to lactate dehydrogenase. Journal Of The American Chemical Society, 114 (21) 7997-8003 doi:10.1021/ja00047a006

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Reference TypeJournal (article/letter/editorial)
TitleRaman spectroscopic studies of the effects of substrate binding on coenzymes bound to lactate dehydrogenase
JournalJournal Of The American Chemical Society
AuthorsDeng, HuaAuthor
Burgner, JohnAuthor
Callender, RobertAuthor
Year1992 (October)Volume114
Issue21
PublisherAmerican Chemical Society (ACS)
DOIdoi:10.1021/ja00047a006Search in ResearchGate
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Mindat Ref. ID1461331Long-form Identifiermindat:1:5:1461331:9
GUID0
Full ReferenceDeng, Hua, Burgner, John, Callender, Robert (1992) Raman spectroscopic studies of the effects of substrate binding on coenzymes bound to lactate dehydrogenase. Journal Of The American Chemical Society, 114 (21) 7997-8003 doi:10.1021/ja00047a006
Plain TextDeng, Hua, Burgner, John, Callender, Robert (1992) Raman spectroscopic studies of the effects of substrate binding on coenzymes bound to lactate dehydrogenase. Journal Of The American Chemical Society, 114 (21) 7997-8003 doi:10.1021/ja00047a006
In(1992, October) Journal Of The American Chemical Society Vol. 114 (21) American Chemical Society (ACS)

See Also

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van Beek, Jeroen, Deng, Hua, Callender, Robert, Burgner, John (2002) Vibrational analysis of NADH cofactors bound to glycerol-3-phosphate dehydrogenase and dogfish lactate dehydrogenase. Journal of Raman Spectroscopy, 33 (5). 397-403 doi:10.1002/jrs.835
Deng, Hua, Zheng, Jie, Burgner, John, Callender, Robert (1989) Hydrogen bonding and reaction specificity in lactate dehydrogenase studied by Raman spectroscopy. The Journal of Physical Chemistry, 93 (12). 4710-4713 doi:10.1021/j100349a007
Deng, H., Zheng, J., Burgner, J., Callender, R. (1989) Molecular properties of pyruvate bound to lactate dehydrogenase: a Raman spectroscopic study. Proceedings of the National Academy of Sciences, 86 (12) 4484-4488 doi:10.1073/pnas.86.12.4484
Deng, Hua, Burgner, John W., Callender, Robert H. (1998) Structure of the Ribonuclease·Uridine−Vanadate Transition State Analogue Complex by Raman Difference Spectroscopy:  Mechanistic Implications. Journal Of The American Chemical Society, 120 (19) 4717-4722 doi:10.1021/ja972824v
Deng, Hua, Callender, Robert (1998) Structure of Dihydrofolate When Bound to Dihydrofolate Reductase. Journal Of The American Chemical Society, 120 (31) 7730-7737 doi:10.1021/ja9814974
Chen, Yong-Qing, van Beek, Jeroen, Deng, Hua, Burgner, John, Callender, Robert (2002) Vibrational Structure of NAD(P) Cofactors Bound to Three NAD(P) Dependent Enzymes:  an Investigation of Ground State Activation. The Journal of Physical Chemistry B, 106 (41). 10733-10740 doi:10.1021/jp025635u
Egawa, Tsuyoshi, Deng, Hua, Chang, Eric, Callender, Robert (2019) Effect of Protein Isotope Labeling on the Catalytic Mechanism of Lactate Dehydrogenase. The Journal of Physical Chemistry B, 123 (46). 9801-9808 doi:10.1021/acs.jpcb.9b08656
Deng, Hua, Vu, Dung V., Clinch, Keith, Desamero, Ruel, Dyer, R. Brian, Callender, Robert (2011) Conformational Heterogeneity within the Michaelis Complex of Lactate Dehydrogenase. The Journal of Physical Chemistry B, 115 (23). 7670-7678 doi:10.1021/jp2015929
Callender, Robert, Deng, Hua, Gilmanshin, Rudolf (1998) Raman difference studies of protein structure and folding, enzymatic catalysis and ligand binding. Journal of Raman Spectroscopy, 29 (1). 15-21 doi:10.1002/(sici)1097-4555(199801)29:1<15::aid-jrs211>3.0.co;2-l
Reddish, Michael J., Peng, Huo-Lei, Deng, Hua, Panwar, Kunal S., Callender, Robert, Dyer, R. Brian (2014) Direct Evidence of Catalytic Heterogeneity in Lactate Dehydrogenase by Temperature Jump Infrared Spectroscopy. The Journal of Physical Chemistry B, 118 (37). 10854-10862 doi:10.1021/jp5050546
Deng, Hua, Lewandowicz, Andrzej, Schramm, Vern L., Callender, Robert (2004) Activating the Phosphate Nucleophile at the Catalytic Site of Purine Nucleoside Phosphorylase:  A Vibrational Spectroscopic Study. Journal Of The American Chemical Society, 126 (31) 9516-9517 doi:10.1021/ja049296p
 
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