Effect of Coenzymes on the Hydrogen-Deuterium Exchange of Chicken Heart Lactic Dehydrogenase as Measured by Infrared Spectrophotometry<sup>*</sup>

Disabato, G; Ottesen, Martin

doi:10.1021/bi00879a007

Cited by 38 publications

(22 citation statements)

References 11 publications

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“…Thus, on the reasonable assumption that for a particular dehydrogenase both the large total hydrophobic free energy change and the contributions to translational and rotational entropic terms are closely similar for NAD' and NADH, it follows that there will be an opposing variation in binding strength and the extent of conformational change. This trend is apparent in the data summarized in Figure 7 both YADH and PHLDH examined in this work and CHL-DH reported in an independent study (DiSabato & Ottesen, 1965). Thus, in all three instances complexation with NAD' is associated with an appreciably larger expenditure of conformational work.…”

Section: = C E -~T K D O~h -L~supporting

confidence: 71%

“…Similar effects have been observed on complex formation of these coenzymes with CHLDH' (DiSabato & Ottesen, 1965), GAPDH' (Zavodsky et al, 1966, and GDH' from bovine liver (Stryker & Parker,1970), suggesting that it is a general characteristic of complexes of dehydrogenases with pyridine nucleotides. in each case, the unequal exchange retardation thus reinforces that the two coenzymes impose specific constraints that lead to quite different conformations.…”

Section: = C E -~T K D O~h -L~supporting

confidence: 54%

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Interdependence of coenzyme-induced conformational work and binding potential in yeast alcohol and porcine heart lactate dehydrogenases: a hydrogen-deuterium exchange study

Weck¹,

Pande²,

Kaegi³

1987

Biochemistry

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Binding of NAD coenzymes to yeast alcohol dehydrogenase (YADH) and porcine heart lactate dehydrogenase (PHLDH) was studied by hydrogen-deuterium exchange with the infrared technique. Conformational changes in the enzymes specific to the coenzymes and their fragments were observed, and the pH dependence of the exchange reaction shows that it conforms to the EX-2 scheme. In both YADH and PHLDH the magnitude of the conformational change of measured by exchange retardation is considerably larger for NAD+ than for NADH. Studies with coenzyme fragments like ADP-ribose, ADP, and AMP also highlight the lack of rigorous correlation between structural features such as charge and size and their influence on exchange behavior. Ternary complexes such as YADH-NAD+-pyrazole, PHLDH-NAD+-oxalate, and PHLDH-NADH-oxamate, which mimic the transition state, have a significantly more pronounced effect on exchange rates than the corresponding binary complexes. The outstanding feature of this study is the demonstration that in the binary enzyme-coenzyme complexes the more loosely bound NAD+ is more effective in retarding exchange than the more firmly bound NADH. These differences are attributed to the unequal structural constraints exerted by the two coenzymes upon the enzymes, which translate to unequal expenditure of transconformational work in the formation of the two complexes. The opposing variation in the free energy of binding and the transconformational work expended can be viewed as an unequal partitioning of the net free energy gain resulting from the protein-ligand interaction into a binding term and that required for conformational change.

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Section: = C E -~T K D O~h -L~supporting

confidence: 71%

Section: = C E -~T K D O~h -L~supporting

confidence: 54%

Interdependence of coenzyme-induced conformational work and binding potential in yeast alcohol and porcine heart lactate dehydrogenases: a hydrogen-deuterium exchange study

Weck¹,

Pande²,

Kaegi³

1987

Biochemistry

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“…The limitation of this method due to the probable formation of an iodine-DPNH complex have already been discussed under Results. It should be added here that conformational modifications occurring in the enzyme upon binding of the coenzyme (Di Sabato and Kaplan, 1964;Di Sabato and Ottesen, 1965;Di Sabato and Kaplan, 1965) could contribute to lessen the binding of iodine in the presence of DPNH.…”

Section: Discussionmentioning

confidence: 99%

“…CHLDH (L-lactate:diphosphopyridine nucleotide (DPN+) oxidoreductase, EC 1.1.1.27), as used in previous studies (Di Sabato and Kaplan, 1963; Di Sabato and Kaplan, 1964;Pesce et al, 1964;Di Sabato and Ottesen, 1965), was obtained as an ammonium sulfate paste as a gift from Dr. N. O. Kaplan, Brandeis University. The paste was dissolved in 0.1 m KC1 or 0.4 m glycine-NaOH buffer, pH 9.45, and dialyzed for about 48 hr at 4°a gainst several changes of the same solvent.…”

Section: Methodsmentioning

confidence: 99%

The Role of the Tyrosyl Groups on the Mechanism of Action of Chicken Heart Lactic Dehydrogenase^*

Sabato¹

1965

Biochemistry

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BIOCHEMISTRY 2288thioester and an associate oxidation-reduction cofactor (e.g., NAD), neither of which is dissociable from the enzyme surface. This proposal would require either two different reversible, direct, stereospecific hydride transfers or one reversible, direct, nonspecific hydride transfer. The direct internal hydride shift proposal is considered most likely at this time since it is analogous with the glyoxalase model system.

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“…In addition the effect of sodium dodecyl sulfate on the exchange rates of these proteins was investigated. This detergent was used by Hvidt et al (1963) to obtain completely deuterated samples of yeast alcohol dehydrogenase and by Di Sabato and Ottesen (1965) for lactic acid dehydrogenase. In these studies the infrared method was used which measures only the exchange of the peptide hydrogens.…”

mentioning

confidence: 99%

Deuterium-Hydrogen Exchange of Muscle Proteins^*

Hartshorne¹,

Stracher²

1965

Biochemistry

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Effect of Coenzymes on the Hydrogen-Deuterium Exchange of Chicken Heart Lactic Dehydrogenase as Measured by Infrared Spectrophotometry^*

Cited by 38 publications

References 11 publications

Interdependence of coenzyme-induced conformational work and binding potential in yeast alcohol and porcine heart lactate dehydrogenases: a hydrogen-deuterium exchange study

Interdependence of coenzyme-induced conformational work and binding potential in yeast alcohol and porcine heart lactate dehydrogenases: a hydrogen-deuterium exchange study

The Role of the Tyrosyl Groups on the Mechanism of Action of Chicken Heart Lactic Dehydrogenase^*

Deuterium-Hydrogen Exchange of Muscle Proteins^*

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Effect of Coenzymes on the Hydrogen-Deuterium Exchange of Chicken Heart Lactic Dehydrogenase as Measured by Infrared Spectrophotometry*

Cited by 38 publications

References 11 publications

Interdependence of coenzyme-induced conformational work and binding potential in yeast alcohol and porcine heart lactate dehydrogenases: a hydrogen-deuterium exchange study

Interdependence of coenzyme-induced conformational work and binding potential in yeast alcohol and porcine heart lactate dehydrogenases: a hydrogen-deuterium exchange study

The Role of the Tyrosyl Groups on the Mechanism of Action of Chicken Heart Lactic Dehydrogenase*

Deuterium-Hydrogen Exchange of Muscle Proteins*

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Product

Resources

About

Effect of Coenzymes on the Hydrogen-Deuterium Exchange of Chicken Heart Lactic Dehydrogenase as Measured by Infrared Spectrophotometry^*

The Role of the Tyrosyl Groups on the Mechanism of Action of Chicken Heart Lactic Dehydrogenase^*

Deuterium-Hydrogen Exchange of Muscle Proteins^*