Molecular changes in the sarcoplasmic reticulum calcium ATPase during catalytic activity

Barth, Andreas; Kreutz, W.; Mäntele, Werner

doi:10.1016/0014-5793(90)80830-c

Cited by 71 publications

(38 citation statements)

References 24 publications

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“…3C), since the photolysis of ADP-[Et(PhNO,)] converted an NO, group to an NO group (Fig. I), and a carbonyl group was formed (Barth et al, 1990(Barth et al, , 1991. These infrared changes represented the background for the measurements performed in the presence of creatine kinase.…”

Section: Resultsmentioning

confidence: 99%

ADP‐Binding and ATP‐Binding Sites in Native and Proteinase‐K‐Digested Creative Kinase, Probed by Reaction‐Induced Difference Infrared Spectroscopy

Raimbault

Clottes

Leydier

et al. 1997

European Journal of Biochemistry

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Conformational changes induced by nucleotide binding to native creatine kinase (CK) from rabbit muscle and to proteinase-K-digested (nicked) CK, were investigated by infrared spectroscopy. Photochemical release of ATP from ATP[Et (PhNO,)] in the presence of creatine and native CK produced reaction-induced difference infrared spectra (RIDS) of CK related to structural changes of the enzyme that paralleled the reversible phosphoryl transfer from ATP to creatine. Similarly the photochemical release of ADP from ADP[Et (PhNO,)] in the presence of phosphocreatine and native CK allowed us to follow the backward reaction and its corresponding RIDS. Infrared spectra of native CK indicated that carboxylate groups of Asp or Glu, and some carbonyl groups of the peptide backbone are involved in the enzymatic reaction. Native and proteinase nicked CK have similar Stokes' radii, tryptophan fluorescence, fluorescence fraction accessible to iodide, and far-ultraviolet CD spectra, indicating that native and modified enzymes have the same quaternary structures. However, infrared data showed that the binding site of the y-phosphate group of the nucleotide was affected in nicked CK compared with that of the native CK.Furthermore, the infrared absorptions associated with ionized carboxylate groups of Asp or Glu amino acid residues were different in nicked CK and in native CK.

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Section: Resultsmentioning

confidence: 99%

ADP‐Binding and ATP‐Binding Sites in Native and Proteinase‐K‐Digested Creative Kinase, Probed by Reaction‐Induced Difference Infrared Spectroscopy

Raimbault

Clottes

Leydier

et al. 1997

European Journal of Biochemistry

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“…The negative bands at 1526-1528cm-' and 1347cm-', and the positive band at 1687 cm-' were readily associated with the photo-products of caged-ADP since the photolysis of caged-ADP converted a NO2 group to a NO, while a new C = O group was formed (Kaplan et al, 1978). The negative 1526-1528-cm-' and 1347-cm-' bands were assigned respectively to the asymmetrical and symmetrical stretching vibration of the nitro group and the positive 1687 cm-' corresponded to the C=O group (Barth et al, 1990(Barth et al, , 1991. The 1687 cm-' ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Changes of Creatine Kinase Secondary Structure Induced by the Release of Nucleotides from Caged Compounds

Raimbault

Buchet

Vial

1996

European Journal of Biochemistry

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Light-induced release of ADP and ATP from their respective caged nucleotides produced small distinct difference infrared spectra of creatine kinase (CK), indicating that ADP and ATP binding to CK promoted different structural alteration. The positive band at 1638-1640 cm-' and the negative band at about 1650-1652 cm on the reaction-induced infrared difference spectra in the amide I region were insensitive to the deuteration effects. They were assigned to the peptide backbone of the ADPIATPbinding site. In addition P, or ATP binding produced another positive band at 1657-1659 cm-' corresponding to the C = O (amide I band) associated with the y-phosphate of ATP. This site was also affected when ADP was added, indicating coupling interactions between both sites. No additional structural changes were observed when creatine and ADP were added, suggesting that the creatine-binding site was uncoupled from the ADP-binding site. The infrared difference spectra of a transition-state-analog complex formed by the addition of ADP, creatine and NO; (a planar-phosphate-mimicking group) lacked the 1657 -1659-cm-' band indicating that the binding site of y-phosphate within CK, was not affected. Infrared changes in the 1560-1590-cm-' region suggested that carboxylate groups of Asp or Glu were involved in the binding of P,, ADP and ATP.

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“…For example, this is possible by using caged-substrates whose light-activated release triggers target activation (e.g. a membrane bound receptor or an ATP driven ion pumps) [21,132,164].…”

Section: Atr-ftir Differences Of Nicotinic Acetylcholine Receptormentioning

confidence: 99%

“…In the case of membrane proteins and photoactive proteins, a variety of systems have been investigated using the approaches described in this review and first introduced for bacteriorhodopsin. A few examples are the photosystem II [116,152], photoactive yellow protein (PYP) [59,118,124,246]; Ca 2+ -ATPase [21,22,52,98,133]; green fluorescent protein (GFP) and potassium channels [92,230]. One measure of the growth of FTIR difference spectroscopy of biomolecules is shown in Fig.…”

Section: Beyond Bacteriorhodopsinmentioning

confidence: 99%

The early development and application of FTIR difference spectroscopy to membrane proteins: A personal perspective

Rothschild

2016

BSI

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Abstract. Membrane proteins facilitate some of the most important cellular processes including energy conversion, ion transport and signal transduction. While conventional infrared absorption provides information about membrane protein secondary structure, a major challenge is to develop a dynamic picture of the functioning of membrane proteins at the molecular level. The introduction of FTIR difference spectroscopy around 1980 to study structural changes in membrane proteins along with a number of associated techniques including protein isotope labeling, site-directed mutagenesis, polarization dichroism, attenuated total reflection and time-resolved spectroscopy have led to significant progress towards this goal. It is now possible to routinely detect conformational changes of individual amino acid residues, backbone peptides, binding ligands, chromophores and even internal water molecules under physiological conditions with time-resolution down to nanoseconds. The advent of ultrafast pulsed-IR lasers has pushed this time-resolution down to femtoseconds. The early development of FTIR difference spectroscopy as applied to membrane proteins with special focus on bacteriorhodopsin is reviewed from a personal perspective.

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Molecular changes in the sarcoplasmic reticulum calcium ATPase during catalytic activity

Cited by 71 publications

References 24 publications

ADP‐Binding and ATP‐Binding Sites in Native and Proteinase‐K‐Digested Creative Kinase, Probed by Reaction‐Induced Difference Infrared Spectroscopy

ADP‐Binding and ATP‐Binding Sites in Native and Proteinase‐K‐Digested Creative Kinase, Probed by Reaction‐Induced Difference Infrared Spectroscopy

Changes of Creatine Kinase Secondary Structure Induced by the Release of Nucleotides from Caged Compounds

The early development and application of FTIR difference spectroscopy to membrane proteins: A personal perspective

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