Alkaline Transition of <i>Rhus vernicifera</i> Stellacyanin, an Unusual Blue Copper Protein

Fernández, Claudio O.; Sannazzaro, Analía Inés; Vila, Alejandro J.

doi:10.1021/bi970504i

Cited by 48 publications

(91 citation statements)

References 41 publications

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“…All the hyperfine shifted resonances follow a Curie temperature dependence, as observed in other Co(II)-substituted blue copper proteins [15,24,25,26,31,32,33,34,35,36,37]. Their chemical shifts and relaxation rates are typical of signals corresponding to proton nuclei from metal ligands ( Table 1).…”

Section: Resultssupporting

confidence: 63%

“…Resonances A and C are broader than the rest of the signals in the spectrum, and exhibit shorter T 1 values (Table 1). Based on these spectral features, we feel confident to assign A and C to the Cys78 b-CH 2 protons by analogy with similar assignments in other Co(II)-substituted cupredoxins [15,24,25,26,31,32,33,34,35,36,37].…”

Section: Resultssupporting

confidence: 60%

“…Paramagnetic NMR investigations on cupredoxins include studies of the native Cu(II) species [19,20,21,22,23] and of their Co(II) and Ni(II) derivatives [15,24,25,26,27,28,29,30,31,32,33,34,35,36,37]. These studies have afforded evidence on the interplay between the strength of the metal-axial ligand interaction and the metal-Cys covalence [15,20,21].…”

Section: Introductionmentioning

confidence: 99%

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Metal-ligand interactions in perturbed blue copper sites: a paramagnetic 1H NMR study of Co(II)-pseudoazurin

et al. 2003

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Pseudoazurin is an electron transfer copper protein, a member of the cupredoxin family. The protein is frequently found in denitrifying bacteria, where it is the electron donor of nitrite reductase. The copper at the active site is coordinated to His40, Cys78, His81 and Met86 in a distorted tetragonal geometry. We have recorded and assigned the (1)H NMR spectra of Co(II)-substituted pseudoazurin from Achromobacter cycloclastes. The (1)H NMR spectrum of Co(II)-pseudoazurin closely resembles that of Co(II)-rusticyanin, reflecting an altered conformation for the Met-Co(II)-Cys moiety in both proteins, compared to Co(II)-azurin, amicyanin and stellacyanin. The electron spin density onto the Sgamma(Cys) is larger in Co(II)-pseudoazurin compared to Co(II)-rusticyanin. Instead, the Co(II)-Met interaction is similar in both derivatives. Hence, the different metal-ligand interactions might be independently modulated by the protein structure. The present work also shows that the electron spin density onto the Co(II)-S(cys) bond is sensibly smaller than the Cu(II)-S(cys). Notwithstanding, NMR data on Co(II)-substituted blue copper proteins can be safely extrapolated to native Cu(II) proteins.

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Section: Resultssupporting

confidence: 63%

Section: Resultssupporting

confidence: 60%

Section: Introductionmentioning

confidence: 99%

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Metal-ligand interactions in perturbed blue copper sites: a paramagnetic 1H NMR study of Co(II)-pseudoazurin

et al. 2003

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“…Native holo N 2 OR has also been widely investigated, and its various copper chromophores (both Cu A and Cu Z ) and their spectroscopic properties have been reported as well as Cu A reconstitution by using Cu(II)(en) 2 SO 4 (49-51). pH titrations of preformed Cu A sites, as well as T1 sites, also results in a perturbation of the copper active site (41,(52)(53)(54)(55)(56). Originally, copper sites were classified as T1, T2, or T3, but the classification scheme was modified with the discovery of Cu A .…”

Section: Discussionmentioning

confidence: 99%

Experimental evidence for a link among cupredoxins: Red, blue, and purple copper transformations in nitrous oxide reductase

Savelieff¹,

Wilson²,

Youssef³

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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The cupredoxin fold is an important motif in numerous proteins that are central to several critical cellular processes ranging from aerobic and anaerobic respiration to catalysis and iron homeostasis. Three types of copper sites have been found to date within cupredoxin folds: blue type 1 (T1) copper, red type 2 (T2) copper, and purple Cu A. Although as much as 90% sequence difference has been observed among some members of this superfamily of proteins that span several kingdoms, sequence alignment and phylogenic trees strongly suggest an evolutionary link and common ancestry. However, experimental evidence for such a link has been lacking. We report herein the observation of pH-dependent transformation between blue T1 copper, red T2 copper, and the native purple Cu A centers of nitrous oxide reductase (N2OR) from Paracoccus denitrificans. The blue and red copper centers form initially before they are transformed into purple Cu A center. This transformation process is pH-dependent, with lower pH resulting in fewer trapped T1 and T2 coppers and faster transition to purple Cu A. These observations suggest that the purple CuA site contains the essential elements of T1 and T2 copper centers and that the Cu A center is preferentially formed at low pH. Therefore, this work provides an underlying link between the various cupredoxin copper sites and possible experimental evidence in vitro for the evolutionary relationship between the cupredoxin proteins. The findings also lend physiological relevance to cupredoxin site biosynthesis.blue type 1 copper ͉ purple copper CuA ͉ red type 2 copper ͉ folding ͉ kinetics

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“…Blue copper proteins show a so-called "alkaline transition" of their absorption wavelength, absorption intensity, and redox potential [91][92][93][94]. With increasing pH, especially at pH 8-11, the absorption maximum at ca.…”

Section: Properties Of Type I Copper In Multicopper Oxidasesmentioning

confidence: 99%

Structure and function of type I copper in multicopper oxidases

Sakurai

Kataoka

2007

Cell. Mol. Life Sci.

128

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Abstract. The type I copper center in multicopper oxidases is constructed from 1Cys2His and weakly coordinating 1Met or the non-coordinating 1Phe/1Leu, and it exhibits spectral properties and an alkaline transition similar to those of the blue copper center in blue copper proteins. Since the type I copper center in multicopper oxidases is deeply buried inside the protein molecule, electron transfers to and from type I copper are performed through specific pathways: the hydrogen bond between an amino acid located at the substrate binding site and a His residue coordinating type I copper, and the His-Cys-His sequence connecting the type I copper center and the trinuclear copper center comprised of a type II copper and a pair of type III coppers. The intramolecular electron transfer rates can be tuned by mutating the fourth ligand of type I copper. Further, mutation at the Cys ligand gives a vacant type I copper center and traps the reaction intermediate during the four-electron reduction of dioxygen.

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Alkaline Transition of Rhus vernicifera Stellacyanin, an Unusual Blue Copper Protein

Cited by 48 publications

References 41 publications

Metal-ligand interactions in perturbed blue copper sites: a paramagnetic 1H NMR study of Co(II)-pseudoazurin

Metal-ligand interactions in perturbed blue copper sites: a paramagnetic 1H NMR study of Co(II)-pseudoazurin

Experimental evidence for a link among cupredoxins: Red, blue, and purple copper transformations in nitrous oxide reductase

Structure and function of type I copper in multicopper oxidases

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