Probing of sulfhydryl groups in the adenosine 5'-diphosphate/adenosine 5'-triphosphate carrier by maleimide spin-labels

Biochemistry ◽  
1987 ◽  
Vol 26 (26) ◽  
pp. 8637-8644 ◽  
Author(s):  
Anton Munding ◽  
Michael Drees ◽  
Klaus Beyer ◽  
Martin Klingenberg
Keyword(s):  
Sulfhydryl Groups ◽  
Spin Labels

Accessibility of protein sulfhydryl groups to nitroxyl spin labels

1997 ◽  
Vol 408-409 ◽  
pp. 177-180 ◽  
Author(s):  
Marianna Török ◽  
Kálmán Hideg ◽  
László Dux ◽  
LászlóI. Horváth
Keyword(s):  
Sulfhydryl Groups ◽  
Spin Labels ◽  
Protein Sulfhydryl ◽  
Protein Sulfhydryl Groups

HISTOCHEMICALLY DEMONSTRABLE SUCCINIC DEHYDROGENASE AND SULFHYDRYL GROUPS IN TISSUES OF ADRENALECTOMIZED RAT

1954 ◽  
Vol 16 (4) ◽  
pp. 315-322 ◽  
Author(s):  
Antti Telkkä ◽  
A. N Kuusisto ◽  
Kimmo K. Mustakallio
Keyword(s):  
Succinic Dehydrogenase ◽  
Sulfhydryl Groups

Iodoacetate inactivation of rape alcohol dehydrogenase

1980 ◽  
Vol 45 (5) ◽  
pp. 1601-1607 ◽  
Author(s):  
Marie Stiborová ◽  
Sylva Leblová
Keyword(s):  
Alcohol Dehydrogenase ◽  
Protein Molecule ◽  
Sulfhydryl Groups ◽  
Inactivation Rate ◽  
First Order ◽  
Ph Dependent ◽  
Kinetics Of

Iodoacetate inactivates rape alcohol dehydrogenase (ADH, EC 1.1.1.1). The inactivation rate follows the kinetics of the first order, is pH-dependent, and decreases below pH 7.5. Besides irreversible alkylation of the sulfhydryl groups of the enzyme iodoacetate also forms a reversible complex with rape ADH. The coenzyme (NAD) and its analogs (ATP, ADP, AMP) competitively protect the enzyme against alkylation; o-phenanthroline also protects the enzyme against alkylation yet noncompetitively with respect to iodoacetate. Imidazole and o-phenanthroline compete with one another for binding to the protein molecule of rape ADH. Whereas o-phenanthroline decreases the inactivation rate imidazole increases the rate of iodoacetate inactivation.

scholarly journals DEER and RIDME Measurements of the Nitroxide-Spin Labelled Copper-Bound Amine Oxidase Homodimer from Arthrobacter Globiformis

2021 ◽  
Author(s):  
Hannah Russell ◽  
Rachel Stewart ◽  
Christopher Prior ◽  
Vasily S. Oganesyan ◽  
Thembaninkosi G. Gaule ◽  
...  
Keyword(s):  
Dipolar Coupling ◽  
Amine Oxidase ◽  
Spin Labels ◽  
Arthrobacter Globiformis ◽  
Copper Amine Oxidase ◽  
Dipole Interactions ◽  
Nitroxide Spin Labels ◽  
Double Electron Electron Resonance ◽  
Dipolar Modulation ◽  
Paramagnetic Centres

AbstractIn the study of biological structures, pulse dipolar spectroscopy (PDS) is used to elucidate spin–spin distances at nanometre-scale by measuring dipole–dipole interactions between paramagnetic centres. The PDS methods of Double Electron Electron Resonance (DEER) and Relaxation Induced Dipolar Modulation Enhancement (RIDME) are employed, and their results compared, for the measurement of the dipolar coupling between nitroxide spin labels and copper-II (Cu(II)) paramagnetic centres within the copper amine oxidase from Arthrobacter globiformis (AGAO). The distance distribution results obtained indicate that two distinct distances can be measured, with the longer of these at c.a. 5 nm. Conditions for optimising the RIDME experiment such that it may outperform DEER for these long distances are discussed. Modelling methods are used to show that the distances obtained after data analysis are consistent with the structure of AGAO.

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