Einzeltreffer — DigiBib

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.

Titel:	Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly.
Autor/in / Beteiligte Person:	Stripp, ST ; Oltmanns, J ; Müller, CS ; Ehrenberg, D ; Schlesinger, R ; Heberle, J ; Adrian, L ; Schünemann, V ; Pierik, AJ ; Soboh, B
Zeitschrift:	The Biochemical journal, Jg. 478 (2021-09-17), Heft 17, S. 3281-3295
Veröffentlichung:	London, UK : Published by Portland Press on behalf of the Biochemical Society, 2021
Medientyp:	academicJournal
ISSN:	1470-8728 (electronic)
DOI:	10.1042/BCJ20210224
Schlagwort:	Carbon Monoxide metabolism Catalytic Domain Disulfides metabolism Electron Spin Resonance Spectroscopy methods Electrons Escherichia coli genetics Ions metabolism Ligands Oxidation-Reduction Protein Binding Spectroscopy, Fourier Transform Infrared methods Spectroscopy, Mossbauer methods Escherichia coli metabolism Escherichia coli Proteins metabolism Hydrogenase metabolism Iron metabolism Iron-Sulfur Proteins metabolism Proteins metabolism Sulfur metabolism
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [Biochem J] 2021 Sep 17; Vol. 478 (17), pp. 3281-3295. MeSH Terms: Escherichia coli / metabolism ; Escherichia coli Proteins / metabolism ; Hydrogenase / metabolism ; Iron / metabolism ; Iron-Sulfur Proteins / metabolism ; Proteins / metabolism ; Sulfur / *metabolism ; Carbon Monoxide / metabolism ; Catalytic Domain ; Disulfides / metabolism ; Electron Spin Resonance Spectroscopy / methods ; Electrons ; Escherichia coli / genetics ; Ions / metabolism ; Ligands ; Oxidation-Reduction ; Protein Binding ; Spectroscopy, Fourier Transform Infrared / methods ; Spectroscopy, Mossbauer / methods References: Proc Natl Acad Sci U S A. 2016 Dec 20;113(51):14722-14726. (PMID: 27930319) ; Eur J Biochem. 1978 Apr 17;85(2):535-47. (PMID: 648533) ; FEBS Lett. 2012 Nov 2;586(21):3882-7. (PMID: 23022438) ; Annu Rev Biochem. 2010;79:507-36. (PMID: 20235826) ; Front Chem. 2021 Jun 14;9:672831. (PMID: 34195174) ; Biochim Biophys Acta. 2013 Aug-Sep;1827(8-9):986-1002. (PMID: 23399489) ; Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt 6):538-41. (PMID: 17554182) ; Front Microbiol. 2018 Jun 12;9:1130. (PMID: 29946299) ; J Biol Chem. 1951 Nov;193(1):265-75. (PMID: 14907713) ; J Am Chem Soc. 2009 Jun 3;131(21):7313-9. (PMID: 19422231) ; J Am Chem Soc. 2020 Jan 22;142(3):1457-1464. (PMID: 31830412) ; J Biol Inorg Chem. 2005 Jun;10(4):417-24. (PMID: 15889286) ; FEBS Lett. 2010 Sep 24;584(18):4109-14. (PMID: 20807532) ; Proc Natl Acad Sci U S A. 1965 Sep;54(3):887-91. (PMID: 4286419) ; Mol Cell. 2007 Jul 6;27(1):29-40. (PMID: 17612488) ; Adv Microb Physiol. 2006;51:1-71. (PMID: 17091562) ; Nature. 2009 Aug 13;460(7257):855-62. (PMID: 19675646) ; Biochim Biophys Acta. 2015 Jun;1853(6):1395-405. (PMID: 25498248) ; J Biol Chem. 2017 Jul 14;292(28):11670-11681. (PMID: 28539366) ; Protein Expr Purif. 2017 Mar;131:109-118. (PMID: 27867058) ; Chem Rev. 2007 Oct;107(10):4206-72. (PMID: 17927159) ; Science. 2007 Nov 30;318(5855):1461-4. (PMID: 18048691) ; J Phys Chem B. 2013 Oct 31;117(43):13523-33. (PMID: 24094065) ; Science. 2017 Sep 1;357(6354):928-932. (PMID: 28860386) ; Biochemistry. 2013 May 14;52(19):3289-96. (PMID: 23597401) ; FEBS Open Bio. 2019 Dec;9(12):2072-2079. (PMID: 31614069) ; Biochem J. 2014 Dec 1;464(2):169-77. (PMID: 25184670) ; Metallomics. 2019 May 22;11(5):925-935. (PMID: 30848269) ; J Biol Chem. 2014 Jul 11;289(28):19364-72. (PMID: 24860091) ; J Mol Biol. 2004 Nov 12;344(1):155-67. (PMID: 15504408) ; Arch Microbiol. 2011 Dec;193(12):893-903. (PMID: 21717143) ; Biochem Biophys Res Commun. 2012 Jul 20;424(1):158-63. (PMID: 22735263) ; Chem Sci. 2015 Aug 1;6(8):4495-4507. (PMID: 29142700) ; J Bacteriol. 1985 Aug;163(2):454-9. (PMID: 3894325) ; Annu Rev Biochem. 1980;49:139-61. (PMID: 6250442) ; FEBS Lett. 2005 Jan 17;579(2):469-72. (PMID: 15642360) ; Structure. 2012 Dec 5;20(12):2124-37. (PMID: 23123111) ; Proc Natl Acad Sci U S A. 2015 Jun 23;112(25):7701-6. (PMID: 26056269) ; Chem Rev. 2014 Apr 23;114(8):4081-148. (PMID: 24655035) ; Biochim Biophys Acta. 2007 Sep;1767(9):1073-101. (PMID: 17692815) ; Eur J Biochem. 1978 Jul 17;88(1):135-41. (PMID: 668704) ; Biochemistry. 1999 May 11;38(19):6335-45. (PMID: 10320364) ; Proc Natl Acad Sci U S A. 2019 Jul 9;116(28):13964-13969. (PMID: 31243147) ; J Bacteriol. 2015 Sep;197(18):2989-98. (PMID: 26170410) ; Nat Chem Biol. 2017 Feb;13(2):147-149. (PMID: 27893704) ; J Biol Chem. 2002 Dec 20;277(51):49945-51. (PMID: 12377778) ; Nature. 1997 Jan 9;385(6612):126. (PMID: 8990114) ; J Biol Chem. 1999 Feb 5;274(6):3331-7. (PMID: 9920874) ; Arch Microbiol. 1992;158(6):444-51. (PMID: 1482271) ; J Biol Chem. 2012 Aug 17;287(34):28409-19. (PMID: 22740694) ; Phys Chem Chem Phys. 2018 Jan 31;20(5):3128-3140. (PMID: 28884175) ; FEBS Lett. 2006 Jul 24;580(17):4065-8. (PMID: 16814778) ; PLoS One. 2014 Sep 11;9(9):e107488. (PMID: 25211029) ; J Mol Microbiol Biotechnol. 2005;10(2-4):181-96. (PMID: 16645314) ; Anal Chem. 2017 Feb 7;89(3):1565-1573. (PMID: 28029041) ; J Biol Chem. 2012 Nov 9;287(46):38845-53. (PMID: 23019332) ; FEBS Lett. 2013 Aug 19;587(16):2512-6. (PMID: 23851071) ; Biochemistry. 2016 Dec 13;55(49):6821-6831. (PMID: 27951644) Contributed Indexing: Keywords: Fe-S proteins; biosynthesis; carbon monoxide; cyanide; maturation; redox activity Substance Nomenclature: 0 (Disulfides) ; 0 (Escherichia coli Proteins) ; 0 (HypC protein, E coli) ; 0 (HypD protein, Bacteria) ; 0 (HypE protein, E coli) ; 0 (Ions) ; 0 (Iron-Sulfur Proteins) ; 0 (Ligands) ; 0 (Proteins) ; 70FD1KFU70 (Sulfur) ; 7U1EE4V452 (Carbon Monoxide) ; E1UOL152H7 (Iron) ; EC 1.12.- (nickel-iron hydrogenase) ; EC 1.12.7.2 (Hydrogenase) Entry Date(s): Date Created: 20210819 Date Completed: 20211203 Latest Revision: 20211214 Update Code: 20231215 PubMed Central ID: PMC8454700

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Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly.