(1,4,7-Tris(4-tert-butyl-2-mercaptobenzyl)-1,4,7-triazacyclononane)iron(III): a model for the iron-sulfur center in nitrile hydratase from Brevibacterium, sp

Beissel, Thomas; Buerger, Kai Silke; Voigt, Gottfried; Wieghardt, Karl; Butzlaff, Christian; Trautwein, Alfred X.

doi:10.1021/ic00054a002

Cited by 71 publications

(68 citation statements)

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“…There are 6 octahedron shows a tetragonal rays. The solid line is a simulation for a diamagnetic system (zero internal field); the parameters are given in Table 2 compression with two shorter RuϪS bonds [Ru(1)ϪS (1) and Ru(1)ϪS(1)Ј].…”

Section: Crystal Structure Determinationmentioning

confidence: 99%

Molecular and Electronic Structure of Two Linear Thiophenolate-Bridged Heterotrinuclear Complexes [LFeRuFeL]2+/3+ (L = 1,4,7-Tris(4-tert-butyl-2-mercaptobenzyl)-1,4,7-triazacyclononane)

Albela

Bill

Brosch

et al. 2000

Eur. J. Inorg. Chem.

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Section: Crystal Structure Determinationmentioning

confidence: 99%

Molecular and Electronic Structure of Two Linear Thiophenolate-Bridged Heterotrinuclear Complexes [LFeRuFeL]2+/3+ (L = 1,4,7-Tris(4-tert-butyl-2-mercaptobenzyl)-1,4,7-triazacyclononane)

Albela

Bill

Brosch

et al. 2000

Eur. J. Inorg. Chem.

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“…250,~ in [Fe([9]aneS3)2] 2*, which is a low-spin diamagnetic complex (Wieghardt, Kiippers & Weiss, 1985). Beissel, Biirger, Voight & Wieghardt (1993) have de- …”

Section: C1 C1 CImentioning

confidence: 99%

Trichloro(1,4,7-trithiacyclononane-S,S',S'')iron(III), [FeCl3(C6H12S3)]

Ballester¹,

Parker²,

Breneman³

1994

Acta Crystallogr C

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“…The structure of the iron center in the active form has been studied by various spectroscopies including ESR (3), resonance Raman (13), extended x-ray absorption fine structure (13) and electron nuclear double resonance (14), and the ligand-donor set of N 3 OS 2 has been proposed (14), which is supported by model complexes of the iron center (15)(16)(17). Recently, the metal site structure has been studied in detail by means of electron nuclear double resonance (18), resonance Raman (19), and x-ray absorption (20) spectroscopies.…”

mentioning

confidence: 99%

Structure of the Photoreactive Iron Center of the Nitrile Hydratase from Rhodococcus sp. N-771

Tsujimura

Dohmae

Odaka

et al. 1997

Journal of Biological Chemistry

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Nitrile hydratase (NHase) from Rhodococcus sp. N-771 is a photoreactive enzyme that is inactivated by nitrosylation of the non-heme iron center and activated by photodissociation of nitric oxide (NO). To obtain structural information on the iron center, we isolated peptide complexes containing the iron center by proteolysis. When the tryptic digest of the ␣ subunit isolated from the inactive form was analyzed by reversed-phase high performance liquid chromatography, the absorbance characteristic of the nitrosylated iron center was observed in the peptide fragment, Asn 105 -Val-Ile-Val-CysSer-Leu-Cys-Ser-Cys-Thr-Ala-Trp-Pro-Ile-Leu-Gly-LeuPro-Pro-Thr-Trp-Tyr-Lys 128 . The peptide contained 0.79 mol of iron/mol of molecule as well as endogenous NO. Subsequently, by digesting the peptide with thermolysin, carboxypeptidase Y, and leucine aminopeptidase M, we found that the minimum peptide segment required for the nitrosylated iron center is the 11 amino acid residues from ␣Ile 107 to ␣Trp 117 . Furthermore, by using mass spectrometry, protein sequence, and amino acid composition analyses, we have shown that the 112th Cys residue of the ␣ subunit is post-translationally oxidized to a cysteine-sulfinic acid (Cys-SO 2 H) in the NHase. These results indicate that the NHase from Rhodococcus sp. N-771 has a novel non-heme iron enzyme containing a cysteine-sulfinic acid in the iron center. Possible ligand residues of the iron center are discussed.Nitrile hydratase (NHase; EC 4.2.1.84) 1 is a bacterial metalloenzyme catalyzing the hydration of nitriles to corresponding amides (1, 2). NHase consists of two kinds of subunits (␣ and ␤ with the molecular mass values of 23 kDa) and contains non-heme iron (3) or non-corrinoid cobalt (4) atoms. The NHase from Rhodococcus sp. N-771, which is a ␣␤ heterodimer containing a non-heme iron, is inactivated by aerobic incubation in the dark for a half-day (dark-inactivation), whereas the enzyme purified from the dark-inactivated cells is immediately converted to the active form by light irradiation (photoactivation) (5, 6). Recently, it has been revealed that dark-inactivation and photoactivation are controlled by association and photodissociation of nitric oxide (NO) with the non-heme iron center (7-9). Similar photosensitivity is observed in the NHases from Rhodococcus sp. N-774 (10) and R312.2 These NHases seem to be identical to the one from Rhodococcus sp. N-771 because of the same nucleotide sequences (11, 12). 3The iron-containing NHase is the first enzyme with a mononuclear low-spin non-heme iron(III) which is thought to be involved in the catalysis (3). The structure of the iron center in the active form has been studied by various spectroscopies including ESR (3), resonance Raman (13), extended x-ray absorption fine structure (13) and electron nuclear double resonance (14), and the ligand-donor set of N 3 OS 2 has been proposed (14), which is supported by model complexes of the iron center (15-17). Recently, the metal site structure has been studied in detail by means of electro...

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(1,4,7-Tris(4-tert-butyl-2-mercaptobenzyl)-1,4,7-triazacyclononane)iron(III): a model for the iron-sulfur center in nitrile hydratase from Brevibacterium, sp

Cited by 71 publications

References 1 publication

Molecular and Electronic Structure of Two Linear Thiophenolate-Bridged Heterotrinuclear Complexes [LFeRuFeL]2+/3+ (L = 1,4,7-Tris(4-tert-butyl-2-mercaptobenzyl)-1,4,7-triazacyclononane)

Molecular and Electronic Structure of Two Linear Thiophenolate-Bridged Heterotrinuclear Complexes [LFeRuFeL]2+/3+ (L = 1,4,7-Tris(4-tert-butyl-2-mercaptobenzyl)-1,4,7-triazacyclononane)

Trichloro(1,4,7-trithiacyclononane-S,S',S'')iron(III), [FeCl3(C6H12S3)]

Structure of the Photoreactive Iron Center of the Nitrile Hydratase from Rhodococcus sp. N-771

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