Evidence for N coordination to Fe in the [2Fe-2S] clusters of Thermus Rieske protein and phthalate dioxygenase from Pseudomonas.

Cline, John F.; Hoffman, Brian M.; Mims, W. B.; LaHaie, E; Ballou, David P.; Fee, James A.

doi:10.1016/s0021-9258(19)83612-8

Cited by 135 publications

(48 citation statements)

References 19 publications

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“…This change in nomenclature is in accordance with the more recent classification of iron-sulfur proteins by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology [16]. The presence of a Rieske [2Fe-2S] center and mononuclear iron in the α subunit of NDO [15,17,18] and all other aromatic ring-hydroxylating dioxygenases is based on biophysical studies with phthalate [19][20][21] and benzene [22,23] dioxygenases and deduced amino acid sequence data [11,24]. NDO was shown to contain ferrous iron as indicated by the identification of a Fe 2+ -nitric oxide complex by electron paramagnetic resonance (EPR) spectroscopy (MD Wolfe, JD Lipscomb, KL and DTG, unpublished data).…”

Section: Introductionmentioning

confidence: 61%

Structure of an aromatic-ring-hydroxylating dioxygenase – naphthalene 1,2-dioxygenase

et al. 1998

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Section: Introductionmentioning

confidence: 61%

Structure of an aromatic-ring-hydroxylating dioxygenase – naphthalene 1,2-dioxygenase

et al. 1998

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“…Biochemical Interpretations of the Interaction of Occupants of the Q0 Site with the [2Fe-2S] Cluster. The recent findings that the [2Fe-2S] clusters in phthalate dioxygenase from Pseudomonas cepacia (Cline et al, 1985), the "Rieske-type" [2Fe-2S] cluster of Thermus thermophilus (Fee et al, 1984), the cyt bcx complexes of R. capsulatus (Gurbiel et al, 1991), and several other organisms (Britt et al, 1991) are probably attached to the polypeptide via two histidines liganded to one of the Fe atoms (Gurbiel et al, 1989(Gurbiel et al, , 1991, provides an attractive possibility for hydrogen bonding from the imidazole NH to the carbonyl oxygen of Q and the phenoxyl of the QH2 or other occupants of the Q0 site (Keske et al, 1990). Similar arrangements have been proposed for the Q0 site (Rich, 1989) and Qb site (Bunker et al, 1982;Wraight, 1982).…”

Section: Discussionmentioning

confidence: 99%

Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: a double-occupancy Qo site model

Ding

Robertson²,

Daldal³

et al. 1992

Biochemistry

206

264

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The ubiquinone complement of Rhodobacter capsulatus chromatophore membranes has been characterized by its isooctane solvent extractability and electrochemistry; we find that the main ubiquinone pool (Qpool) amounts to about 80% of the total ubiquinone and has an Em7 value close to 90 mV. To investigate the interactions of ubiquinone with the cyt bc1 complex, we have examined the distinctive EPR line shapes of the [2Fe-2S] cluster of the cyt bc1 complex when the Qpool-cyt bc1 complex interactions are modulated by changing the numbers of Q or QH2 present (by solvent extraction and reconstitution), by the exposure of the [2Fe-2S] to the Qpool in different redox states, by the presence of inhibitors specific for the Qo site (myxothiazol and stigmatellin) and Qi site (antimycin), and by site-specific mutations of side chains of the cyt b polypeptide (mutants F144L and F144G) previously identified as important for Qo site structure. Evidence suggests that the Qo site can accommodate two ubiquinone molecules. One (designated Qos) is bound relatively strongly and is second only to the ubiquinone of the QA site of the reaction center in its resistance to solvent extraction. In this strong interaction, the Qo site binds Q and QH2 with approximately equal affinities. Their bound states are distinguished by their effects on the [2Fe-2S] cluster spectral feature at gx at 1.783 (Q) and gx at 1.777 (QH2); titration of the line-shape change reveals an Em7 value of approximately 95 mV. The other molecule (Qow) is bound more weakly, in the same range as the ubiquinone of the QB site of the reaction center. Again, the affinities of the Q form (gx at 1.800) and QH2 form (gx at 1.777) are nearly equal, and the Em7 value measured is approximately 80 mV. These results are discussed in terms of earlier EPR analyses of the cyt bc1 complexes of other systems. A Qo site double-occupancy model is considered that builds on the previous model based on Qo site mutants [Robertson, D. E., Daldal, F.,& Dutton, P. L. (1990) Biochemistry 29, 11249-11260] and includes the recent suggestion that two of the [2F3-2S] cluster ligands of the R. capsulatus cyt bc1 complex are histidines [Gurbiel, R. J. Ohnishi, T., Robertson, D. E. Daldal, F., & Hoffman, B. M. (1991) Biochemistry 30, 11579-11584]. We speculate that the cyt bc1 complex complexes a full enzymatic turnover without necessary exchange of ubiquinone with the Qpool.

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“…In accord with this role, in the crystal structures of the bovine and chicken cytochrome bc 1 complex (Xia et al, 1997;Berry et al, 1997) the Rieske protein occupies a position intermediate between cytochrome b and cytochrome c 1 . Site-directed mutagenesis studies (Davidson et al, 1992) and spectroscopic examination of site-specific, isotopesubstituted Rieske-type proteins (Cline et al, 1985;Gurbiel et al, 1996) led to the general conclusion that the novel EPR spectrum of the Rieske center (Rieske et al, 1964) originates from unique structural features of the Fe/S cluster, in which one iron is coordinated to two cysteine and the other iron is coordinated to two histidine residues: (Cys-S-) 2 [2Fe-2S](-N-His) 2 . A high-resolution, three-dimensional X-ray structure of the water-soluble fragment of the bovine Rieske iron-sulfur protein, which confirms the predictions of the spectroscopic and mutagenesis studies, was described recently by Michel and coworkers (Iwata et al, 1996; see also Zhang et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Untitled

Gatti

Tarr

Fee

et al. 1998

Journal of Bioenergetics and Biomembranes

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The structural gene encoding the Rieske iron-sulfur protein from Thermus thermophilus HB8 has been cloned and sequenced. The gene encodes a protein of 209 amino acids that begins with a hydrophilic N-terminus followed by a stretch of 21 hydrophobic amino acids that could serve as a transmembrane helix. The remainder of the protein has a hydrophobicity pattern typical of a water-soluble protein. A phylogenetic analysis of 26 Rieske proteins that are part of bc1 or b6f complexes shows that they fall into three major groups: eubacterial and mitochondrial, cyanobacterial and plastid, and five highly divergent outliers, including that of Thermus. Although the overall homology with other Rieske proteins is very low, the C-terminal half of the Thermus protein contains the signature sequence CTHLGC-(13X)-CPCH that most likely provides the ligands of the [2Fe-2S] cluster. It is proposed that this region of the protein represents a small domain that folds independently and that the encoding DNA sequence may have been transferred during evolution to several unrelated genes to provide the cluster attachment site to proteins of different origin. The role of individual residues in this domain of the Thermus protein is discussed vis-a-vis the three-dimensional structure of the bovine protein (Iwata et al., 1996 Structure 4, 567-579).

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Evidence for N coordination to Fe in the [2Fe-2S] clusters of Thermus Rieske protein and phthalate dioxygenase from Pseudomonas.

Cited by 135 publications

References 19 publications

Structure of an aromatic-ring-hydroxylating dioxygenase – naphthalene 1,2-dioxygenase

Structure of an aromatic-ring-hydroxylating dioxygenase – naphthalene 1,2-dioxygenase

Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: a double-occupancy Qo site model

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