Dallas G. Cross Publications


Hydrogen-deuterium exchange in nucleosides and nucleotides. Mechanism for exchange of the exocyclic amino hydrogens of adenosine

DG Cross, Allister Brown , Harvey F. Fisher; Biochemistry, 1975, 14 (12), pp 2745-2749 DOI: 10.1021/bi00683a029 Publication Date: June 1975 ABSTRACT: The pH dependence of the apparent first-order rate constant for the exchange of the exocyclic amino hydrogens of adenosine with deuterium from the solvent was measured by stopped-flow ultraviolet spectroscopy. This dependence shows ...
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The Mechanism of Glutamate Dehydrogenase Reaction III. THE BINDING OF LIGANDS AT MULTIPLE SUBSITES AND RESULTING KINETIC EFFECTS

DG Cross, HF Fisher - Journal of Biological Chemistry, 1970 - ASBMB ABSTRACT: Differential spectroscopic studies of complexes between glutamate dehydrogenase and its various substrates, reaction products, cofactors, regulatory nucleotides, and analogues of these compounds have permitted direct observation of the interactions of ...
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Catalytic activity of sub-units of glutamic dehydrogenase

HF Fisher, DG Cross, LL McGREGOR - 1962 - nature.com L-GLUTAMIC dehydrogenase (GDH) has been shown to dissociate into sub-units under a variety of experimental conditions, such as dilution 1, high or low pH 2, 3, and presence of DPNH 4, urea 5, diethylstilbœstrol 6, or bicarbonate ions 7. The relationship between the ...
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Dehydrogenase-reduced coenzyme difference spectra, their resolution, and relation to the stereospecificity of hydrogen transfer

HF Fisher, DL Adija, DG Cross - Biochemistry, 1969 - ACS Publications ABSTRACT: The binding of reduced diphosphopyridine nucleotide to any specific
dehydrogenase causes changes in the ultraviolet absorption spectrum of the reduced
coenzyme. The 340-mp regions of the resulting difference spectra can all be resolved into ...
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Ultraviolet spectrophotometric characterization of a glutamate dehydrogenase-reduced coenzyme-α-ketoglutarate complex

DG Cross - Journal of Biological Chemistry, 1972 - ASBMB ABSTRACT: Glutamate dehydrogenase binds α-ketoglutarate and TPNH in a ternary complex such that both ligands are more tightly bound than in binary complexes. TPNH, bound in this ternary complex, absorbs maximally at 332 nm with E 332= 5.2 mM-1 cm-1 in contrast to ...
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Conformation and conformational changes of reduced diphosphopyridine nucleotide in solution

DG Cross, HF Fisher - Biochemistry, 1969 - ACS Publications ABSTRACT: The binding of reduced diphosphopyridine nucleotide to dehydrogenases can produce changes in its ultraviolet spectrum attributable to both the reduced nicotinamide and adenine moieties. Changes in coenzyme conformation have been proposed to ...
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Two-step binding of adenosine diphosphate to L-glutamate dehydrogenase. Effect on the binding of reduced nicotinamide adenine diphosphate and on enzymic catalysis

AH Colen, DG Cross, HF Fisher - Biochemistry, 1974 - ACS Publications ABSTRACT: Studies of the binding of NADPH and ADP to L-glutamate dehydrogenase by both difference spectroscopic and gel filtration methods demonstrate that a ternary complex can be formed with a negative heterotropic binding cooperativity of 6.8. The difference ...
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The role of tyrosyl-hydrogen bonds in the quaternary structure of the glutamate dehydrogenase molecule

HF Fisher, LL McGregor, DG Cross - Biochimica et Biophysica Acta, 1962 - Elsevier Cited by 23 Related articles All 2 versions Cite Save aHF Fisher, DG Cross - Biochemical and Biophysical Research ... , 1965 - Academic Press
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Enzyme-Coenzyme Complexes of Pyridine Nucleotide-Linked Dehydrogenases

HF Fisher, DG Cross - Science, 1966 - sciencemag.org ABSTRACT: Enzyme-reduced coenzyme binary complexes produce previously unreported shifts in the spectrum of the free coenzyme. These shifts give rise to difference spectra which resemble a general environmental change for reduced diphosphopyridine nucleotide ( ...
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Hydrogen exchange in nucleosides and nucleotides. Measurement of hydrogen exchange by stopped-flow and ultraviolet difference spectroscopy

DG Cross - Biochemistry, 1975 - ACS Publications ABSTRACT: Time-dependent changes in the ultraviolet absorbance of the adenine chromophore are observed in the stopped-flow spectrophotometer when adenosine and its analogs are rapidly transferred from protium oxide to deuterium oxide. These absorbance ...



Hydrogen exchange at the amide group of reduced pyridine nucleotides and the inhibition of that reaction by dehydrogenases.

DG Cross, A Brown, HF Fisher - Journal of Biological Chemistry, 1976 - ASBMB ABSTRACT: Stopped flow ultraviolet spectroscopy has been used to measure the rate of hydrogen exchange with solvent at the amide group of reduced nicotinamide nucleotide coenzymes. Several mechanisms for the exchange reaction are considered in the light of ...

Hydrogen exchange at the amide group of reduced pyridine nucleotides and the inhibition of that reaction by dehydrogenases.

HF Fisher, RE Gates, DG Cross - Nature, 1970 - ncbi.nlm.nih.gov 1. Nature. 1970 Oct 17;228(5268):247-9. A ligand exclusion theory of allosteric effects. Fisher HF, Gates RE, Cross DG. PMID: 5479521 [PubMed - indexed for MEDLINE]. MeSH Terms. Binding Sites*; Catalysis; Chemical Phenomena; ...
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Hydrogen-deuterium exchange in nucleosides and nucleotides. Mechanism for exchange of the exocyclic amino hydrogens of adenosine

DC Cross, A Brown, HF Fisher - Biochemistry, 1975 - ACS Publications ABSTRACT: The pH dependence of the apparent first-order rate constant for the exchange of the exocyclic amino hydrogens of adenosine with deuterium from the solvent was measured by stopped-flow ultraviolet spectroscopy. This dependence shows acid ...
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The Spatial Location of Chromophoric Residues in L-Glutamate Dehydrogenase*

DG Cross, HF Fisher - Biochemistry, 1966 - ACS Publications ABSTRACT: Solvent perturbation difference spectroscopy was used to show the spatial location of tyrosyl, tryptophyl, and phenylalanyl residues in L-glutamate dehydrogenase. It was found that: 58% of the tyrosyl, 22% of the tryptophyl, and 75% of the phenylalanyl ...
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Spectrophotometric studies of the quaternary structure of proteins: I. Method of concentration-difference spectra

HF Fisher, DG Cross - Archives of Biochemistry and Biophysics, 1965 - Elsevier ABSTRACT: A method is presented for determining effects of concentration-dependent structural changes on environment of chromophoric residues of proteins. The theory for this technique of "concentration-difference spectra" is developed; the experimental methods required for ...
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Spectrophotometric studies of the quaternary structure of proteins: II. The α, β split of glutamic dehydrogenase

DG Cross, HF Fisher - Archives of biochemistry and biophysics, 1965 - Elsevier ABSTRACT: The method of "concentration-difference spectra" was used to study the α, β (dilution) dissociation of the glutamic dehydrogenase molecule. It was found that no phenylalanyl, tryptophanyl, or tyrosyl residues undergo a change in environment in the ...



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