The Cofactor of the Iron–Sulfur Cluster Free Hydrogenase Hmd: Structure of the Light‐Inactivation Product

Shima, Seigo; Lyon, Erica J.; Sordel-Klippert, Melanie; Kauss, Manuela; Kahnt, Jörg; Thauer, Rudolf K.; Steinbach, K; Xie, Xiulan; Verdier, Laurent; Griesinger, Christian

doi:10.1002/ange.200353763

Cited by 64 publications

(43 citation statements)

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“…However, it was shown later that the active site includes a single iron atom with an unusual coordination sphere. [24,[39][40][41] Above all, [FeFe] hydrogenase has been considered to be mainly a H 2 producer and demonstrates considerably higher turnover numbers and frequencies for H 2 production relative to the other hydrogenases. [21,22,42] A representative example of these enzymes was isolated from Desulfovibrio desulfuricans.…”

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confidence: 99%

Diiron Dichalcogenolato (Se and Te) Complexes: Models for the Active Site of [FeFe] Hydrogenase

et al. 2011

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Keywords: Iron / Selenium / Tellurium / Hydrogenases / Electrocatalysis A short overview of diiron dichalcogenolato (Se and Te) model complexes related to the chemistry of the diiron subsite of [FeFe] hydrogenase is presented. These model complexes allow direct comparison with the diiron dithiolato compound analogues for their ability to catalyze the formation of H 2 from weak acids. Few detailed photoelectron spec-

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Section: Introductionmentioning

confidence: 99%

Diiron Dichalcogenolato (Se and Te) Complexes: Models for the Active Site of [FeFe] Hydrogenase

et al. 2011

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“…It is this feature of these enzymes that gives the class its name (Shima et al 2004). Fe-S cluster-free hydrogenases (also referred to as [Fe]-hydrogenases: Armstrong and Albracht 2005) are found only in a small group of methanogenic archaea and function as hydrogenforming methylenetetrahydromethanopterin dehydrogenases (Hmd).…”

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Maturation of [NiFe]-hydrogenases in Escherichia coli

2007

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Hydrogenases catalyze the reversible oxidation of dihydrogen. Catalysis occurs at bimetallic active sites that contain either nickel and iron or only iron and the nature of these active sites forms the basis of categorizing the enzymes into three classes, the [NiFe]-hydrogenases, the [FeFe]-hydrogenases and the iron sulfur cluster-free [Fe]-hydrogenases. The [NiFe]-hydrogenases and the [FeFe]-hydrogenases are unrelated at the amino acid sequence level but the active sites share the unusual feature of having diatomic ligands associated with the Fe atoms in the these enzymes. Combined structural and spectroscopic studies of [NiFe]-hydrogenases identified these diatomic ligands as CN- and CO groups. Major advances in our understanding of the biosynthesis of these ligands have been achieved primarily through the study of the membrane-associated [NiFe]-hydrogenases of Escherichia coli. A complex biosynthetic machinery is involved in synthesis and attachment of these ligands to the iron atom, insertion of the Fe(CN)2CO group into the apo-hydrogenase, introduction of the nickel atom into the pre-formed active site and ensuring that the holoenzyme is correctly folded prior to delivery to the membrane. Although much remains to be uncovered regarding each of the individual biochemical steps on the pathway to synthesis of a fully functional enzyme, our understanding of the initial steps in CN- synthesis have revealed that it is generated from carbamoyl phosphate. What is becoming increasingly clear is that the metabolic origins of the carbonyl group may be different.

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“…[14] Light inactivation is associated with the bleaching of the cofactors color and the release of one iron atom [14] and most probably two CO molecules. [15] The active cofactor is also temperature-sensitive: [13] it is inactivated at 50 8C, with a half-life of only a few minutes. The half-life increases to approximately 60 minutes in the presence of 10 mm 2-thioethanol.…”

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“…The holoenzyme was found to contain two moles of CO per mole of Fe by FTIR analysis and 2.4 AE 0.2 moles of CO per mole of Fe by chemical analysis. [15] Upon incubation of the inactivated cofactor (542 Da compound) for 60 min at 37 8C with phosphodiesterase I (0.07 U Crotalus adamanteus Venom from Amersham Bioscience, Freiburg, plus 40 mmol inactived cofactor in 50 mL 100 mm Gly/NaOH pH 8.9 containing 100 mm NaCl and 14 mm MgCl 2 ) two main products were formed that are referred to as 363 Da and 197 Da. containing sodium (23 Da) or lithium (7 Da) ions. The intensity of the signal at 498 Da increased with increasing CID voltage.…”

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confidence: 99%

“…The 13 C NMR signals attributed to C(4'), C(5'), C(c), C(d), C(e), and C(i) were split through J couplings with 31 P, while for the C(i)H 3 and the C(j)H 3 protons a strong and a weak 31 P, 1 H HMBC interaction was observed, respectively (Scheme 2 and Figure 4). The protons of C(g) showed HMBC correlations with N(a) after 15 N-labeling of the cofactor. The N(1) and N(2) atoms of the GMP moiety were assigned through HSQC cross peaks with their directly bound protons.…”

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