scholarly journals Mechanistic Insights into Dissolved Organic Sulfur Photomineralization through the Study of Cysteine Sulfinic Acid

2020 ◽  
Vol 54 (20) ◽  
pp. 13066-13076
Author(s):  
Rachele Ossola ◽  
Baptiste Clerc ◽  
Kristopher McNeill
Keyword(s):  
Organic Sulfur ◽  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid

scholarly journals MOLECULAR MECHANISM OF THE REDUCTION OF CYSTEINE SULFINIC ACID OF PEROXIREDOXIN TO CYSTEINE BY MAMMALIAN SULFIREDOXIN

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Sue Goo Rhee ◽  
Woojin Jeong ◽  
Sung Jun Park ◽  
Tong‐Shin Chang ◽  
Duck Yeon Lee
Keyword(s):  
Molecular Mechanism ◽  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid

Microassay of cysteine sulfinic acid by an enzymatic cycling method

1980 ◽  
Vol 101 (2) ◽  
pp. 288-293 ◽  
Author(s):  
Akemichi Basa ◽  
Satoru Yamagami ◽  
Hiroyuki Mizuo ◽  
Heitaroh Iwata
Keyword(s):  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid ◽  
Enzymatic Cycling

scholarly journals Chemical proteomics reveals new targets of cysteine sulfinic acid reductase

2018 ◽  
Vol 14 (11) ◽  
pp. 995-1004 ◽  
Author(s):  
Salma Akter ◽  
Ling Fu ◽  
Youngeun Jung ◽  
Mauro Lo Conte ◽  
J. Reed Lawson ◽  
...  
Keyword(s):  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid ◽  
Chemical Proteomics ◽  
New Targets

scholarly journals Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester Intermediate

2008 ◽  
Vol 283 (35) ◽  
pp. 23846-23851 ◽  
Author(s):  
Thomas J. Jönsson ◽  
Michael S. Murray ◽  
Lynnette C. Johnson ◽  
W. Todd Lowther
Keyword(s):  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid

scholarly journals Substrate and Cofactor Range Differences of Two Cysteine Dioxygenases from Ralstonia eutropha H16

2015 ◽  
Vol 82 (3) ◽  
pp. 910-921 ◽  
Author(s):  
Leonie Wenning ◽  
Nadine Stöveken ◽  
Jan Hendrik Wübbeler ◽  
Alexander Steinbüchel
Keyword(s):  
Ralstonia Eutropha ◽  
Metal Chelate ◽  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid ◽  
Content Type ◽  
Apparent Homogeneity ◽  
Metal Cofactor ◽  
Metal Chelate Affinity Chromatography

ABSTRACTCysteine dioxygenases (Cdos), which catalyze the sulfoxidation of cysteine to cysteine sulfinic acid (CSA), have been extensively studied in eukaryotes because of their roles in several diseases. In contrast, only a few prokaryotic enzymes of this type have been investigated. InRalstonia eutrophaH16, two Cdo homologues (CdoA and CdoB) have been identified previously.In vivostudies showed thatEscherichia colicells expressing CdoA could convert 3-mercaptopropionate (3MP) to 3-sulfinopropionate (3SP), whereas no 3SP could be detected in cells expressing CdoB. The objective of this study was to confirm these findings and to study both enzymes in detail by performing anin vitrocharacterization. The proteins were heterologously expressed and purified to apparent homogeneity by immobilized metal chelate affinity chromatography (IMAC). Subsequent analysis of the enzyme activities revealed striking differences with regard to their substrate ranges and their specificities for the transition metal cofactor, e.g., CdoA catalyzed the sulfoxidation of 3MP to a 3-fold-greater extent than the sulfoxidation of cysteine, whereas CdoB converted only cysteine. Moreover, the dependency of the activities of the Cdos fromR. eutrophaH16 on the metal cofactor in the active center could be demonstrated. The importance of CdoA for the metabolism of the sulfur compounds 3,3′-thiodipropionic acid (TDP) and 3,3′-dithiodipropionic acid (DTDP) by further converting their degradation product, 3MP, was confirmed. Since 3MP can also function as a precursor for polythioester (PTE) synthesis inR. eutrophaH16, deletion ofcdoAmight enable increased synthesis of PTEs.

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