Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching.

Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching. Research Abstract Details 

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Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching. Abstract Text:

H Miyata,H Asai,

The features of the charge distribution in the vicinity of the ATP-binding site of heavy meromyosin (HMM) were investigated by the technique of dynamic fluorescence quenching. Instead of ATP, 1,N6-ethenoadenosine triphosphate (epsilon-ATP), a fluorescent derivative of ATP, was attached to the ATP-binding site in the presence of an ATP-regenerating system. The I- ion and acrylamide were used as negative- and zero-charged quenchers. In addition to these quenchers, we used the TI+ ion, which has recently been found to be a highly efficient quencher with positive charge, and to be generally applicable to fluorescence-labeled proteins. The Stern-Volmer quenching constants of TI+ and I- for epsilon-ATP bound to HMM both decreased with increasing ionic strength of the solvent. This result means that there is an electrostatic attractive force between the fluorophore ad both TI+ and I-. On the other hand, the Stern-Volmer quenching constant of acrylamide was not significantly affected by a change in ionic strength. This result confirms that no significant change in protein conformation in the vicinity of the epsilon-ATP-binding site of HMM occurs with change in ionic strength. In order to interpret these results, we propose a model in which a positive charge is located on one side of the epsilon-adenine ring and a negative charge is located on the opposite side. The negative charge is attributed to the phosphate group in epsilon-ATP and positive one is probably attributable to a lysyl residue in the polypeptide chain of HMM.

Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching. Publishing Authors By Initials

H Miyata,H Asai,

For similar investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research abstracts see: investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research

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Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 90

Page Numbers: 133-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1981

Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching. Keywords Mesh Terms:

KEYWORDS: Spectrometry, Fluorescence

MESH TERMS: metabolism

Chemical & Substance for Abstract: Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching. Information

Substance Name: Adenosine Triphosphate

Registry Number: 56-65-5

Grant and Affiliation Information for Amphoteric charge distribution at the enzymatic site of 1,N6-ethenoadenosine triphosphate-binding heavy meromyosin determined by dynamic fluorescence quenching.

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Country: JAPAN

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MEDLINETA: J Biochem

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