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Title (Primary) Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly
Author Stripp, S.T.; Oltmanns, J.; Müller, C.S.; Ehrenberg, D.; Schlesinger, R.; Heberle, J.; Adrian, L.; Schünemann, V.; Pierik, A.J.; Soboh, B.
Journal Biochemical Journal
Year 2021
Department UBT
Volume 478
Issue 17
Page From 3281
Page To 3295
Language englisch
Topic T7 Bioeconomy
Supplements https://port.silverchair-cdn.com/port/content_public/journal/biochemj/478/17/10.1042_bcj20210224/1/bcj-2021-0224_supp.pdf?Expires=1634222199&Signature=jl8bcEjPbxTzMGgY4slDiwwbS-OgS5ElzgK1h0FzcO9duD01dpWWE6auBbQQ1XWqnUargrI-4Xk1Vlgjw-TTEUp~CVQCqFBtcaoHFfR1LnzkTrXJLolz~j2wIuNrHMoVysDECXq90LiyL6i9LO5or2WWgxve4aSSyAnOnUwnph44Ng7iO193WilmdTZy-HFab1BaAey6~GlO1Bvy0HcUx4SbDfHUG8tLJ0pTyXjT-KgYAI0z7t-85-cS-UtQuzn9W5MSuZ96fjIev6csmisW7M2ZkU1cOD7KCv2wkO5ivnSZMWQqThugSyHdEBTbFnk2tCtalRHnWJ67wdSwRMuTlA__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA
Keywords biosynthesis, carbon monoxide, cyanide, Fe-S proteins, maturation, redox activity
UFZ wide themes ProVIS;
Abstract The [4Fe-4S] cluster containing scaffold complex HypCD is the central construction site for the assembly of the [Fe](CN)2CO cofactor precursor of [NiFe]-hydrogenase. While the importance of the HypCD complex is well established, not much is known about the mechanism by which the CN- and CO ligands are transferred and attached to the iron ion. We report an efficient expression and purification system producing the HypCD complex from E. coli with complete metal content. This enabled in-depth spectroscopic characterizations. The results obtained by EPR and Mössbauer spectroscopy demonstrate that the [Fe](CN)2CO cofactor and the [4Fe-4S] cluster of the HypCD complex are redox active. The data indicate a potential-dependent interconversion of the [Fe]2+/3+ and [4Fe-4S]2+/+ couple, respectively. Moreover, ATR FTIR spectroscopy reveals potential-dependent disulfide formation, which hints at an electron confurcation step between the metal centers. MicroScale thermophoresis indicates preferable binding between the HypCD complex and its in vivo interaction partner HypE under reducing conditions. Together, these results provide comprehensive evidence for an electron inventory fit to drive multi-electron redox reactions required for the assembly of the CN- and CO ligands on the scaffold complex HypCD.
Persistent UFZ Identifier https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=25100
Stripp, S.T., Oltmanns, J., Müller, C.S., Ehrenberg, D., Schlesinger, R., Heberle, J., Adrian, L., Schünemann, V., Pierik, A.J., Soboh, B. (2021):
Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly
Biochem. J. 478 (17), 3281 - 3295