caa a22 4500 378859013 CHVBK 20180305123341.0 cr unu---uuuuu 161128e20031107xx s 000 0 eng 10.1515/BC.2003.163 doi (NATIONALLICENCE)gruyter-10.1515/BC.2003.163 Molecular Recognition between Azotobacter vinelandii Rhodanese and a Sulfur Acceptor Protein [Elektronische Daten] [A. Cereda, F. Forlani, S. Iametti, R. Bernhardt, P. Ferranti, G. Picariello, S. Pagani, F. Bonomi] The occurrence of rhodanese-like proteins in the major evolutionary phyla, together with the observed abundance of these proteins also within the same genome, suggests that their function cannot be limited to cyanide scavenging. The aim of the present study was to investigate whether Azotobacter vinelandii RhdA, an enzyme possessing unique biochemical and structural features with respect to other members of rhodanese homology superfamily, could recognize a suitable protein as a potential acceptor of the sulfane sulfur held on its catalytic Cys residue. Both the potential sulfur-delivery RhdA-S and the sulfur- deprived RhdA were found to interact with either holo- or apo-adrenodoxin, the 'substrate' protein used in this work. Interaction of RhdA-S with apoadrenodoxin led to mobilization of RhdA-S sulfane sulfur. Under appropriate conditions, the sulfur released from RhdA-S was productively used for 2Fe 2S cluster reconstitution to yield holo-adrenodoxin from apo-adrenodoxin in the absence of any other sulfur source. A comparison of the reactivity of RhdA-S with protein and non-protein thiols allowed also some insights into the accessibility of the sulfane sulfur carried by RhdA. Copyright © 2003 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Cereda A. aut Forlani F. aut Iametti S. aut Bernhardt R. aut Ferranti P. aut Picariello G. aut Pagani S. aut Bonomi F. aut Biological Chemistry Walter de Gruyter 384/10-11(2003-11-07), 1473-1481 1431-6730 384:10-11<1473 2003 384 bchm https://doi.org/10.1515/BC.2003.163 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2003.163 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Cereda A. aut NATIONALLICENCE 700 1- Forlani F. aut NATIONALLICENCE 700 1- Iametti S. aut NATIONALLICENCE 700 1- Bernhardt R. aut NATIONALLICENCE 700 1- Ferranti P. aut NATIONALLICENCE 700 1- Picariello G. aut NATIONALLICENCE 700 1- Pagani S. aut NATIONALLICENCE 700 1- Bonomi F. aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 384/10-11(2003-11-07), 1473-1481 1431-6730 384:10-11<1473 2003 384 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter