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 apo-adrenodoxin 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.

Molecular recognition between Azotobacter vinelandii rhodanese and a sulfur acceptor protein / A. Cereda, F. Forlani, S. Iametti, R. Bernhardt, P. Ferranti, G. Picariello, S. Pagani, F. Bonomi. - In: BIOLOGICAL CHEMISTRY. - ISSN 1431-6730. - 384:10-11(2003), pp. 1473-1481.

Molecular recognition between Azotobacter vinelandii rhodanese and a sulfur acceptor protein

A. Cereda
Primo
;
F. Forlani
Secondo
;
S. Iametti;S. Pagani
;
F. Bonomi
Ultimo
2003

Abstract

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 apo-adrenodoxin 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.
Adrenodoxin; Azotobacter vinelandii RhdA; Iron-sulfur cluster assembly; Molecular interaction; Sulfur release; Sulfurtransferases
Settore BIO/10 - Biochimica
http://hdl.handle.net/2434/179106
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/254728
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