Refined crystal structure of pseudoazurin from Methylobacterium extorquens AM1 at 1.5 Å resolution

Inoue, Takahiro; Yu, Kai; Harada, S.; Kasai, Nobutami; Ohshiro, Yu; Suzuki, Shuichi; Kohzuma, Takamitsu; Tobari, Jiro

doi:10.1107/s0907444994000260

Cited by 34 publications

(34 citation statements)

References 5 publications

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“…More recently, the x-ray structure of pseudoazurin from A. cycloclastes has been reported ( Fig. 1) (16), and the structure is almost identical to that of pseudoazurin from A. faecalis (11,12) and Pseudomonas AM1 (17).…”

Section: ؊1mentioning

confidence: 68%

Spectroscopic and Electrochemical Studies on Active-site Transitions of the Type 1 Copper Protein Pseudoazurin from Achromobacter cycloclastes

Kohzuma

Dennison

McFarlane

et al. 1995

Journal of Biological Chemistry

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The single type 1 copper protein pseudoazurin from Achromobacter cycloclastes gives reversible electrochemical behavior at a (4-pyridyl)disulfide-modified gold electrode. Measurements carried out at 25.0°C indicate a midpoint reduction potential of E1 ⁄2 ‫؍‬ 260 mV versus normal hydrogen electrode at pH 7.0 and a peakto-peak separation of ⌬E p ‫؍‬ 59 mV. The diffusion coefficient and heterogeneous electron transfer rate constant are estimated to be 2.23 ؋ 10 ؊6 cm 2 s ؊1 and 3.7 ؋ 10 ؊2 cm s ؊1 , respectively. Also, controlled potential electrolysis indicates a 1-electron transfer process and a formal reduction potential of 259 mV versus normal hydrogen electrode for the Cu(II)/Cu(I) couple. The heterogeneous electron transfer rate constant determined at the (4-pyridyl)disulfide-modified gold electrode at pH 4.6 is 6.7 ؋ 10 ؊3 cm s ؊1, consistent with a slower process at the positively charged electrode surface. At pH 11.3, UVvisible, EPR, and resonance Raman spectra indicate a conversion of the distorted tetrahedral copper geometry to a trigonal structure. The trigonal form has elongated axial bonding and an axial EPR spectrum. At pH 11.3, the reduction potential is further decreased, and Cu-S bands in resonance Raman spectra at 330 -460 cm ؊1 are shifted to higher energy (ϳ10 cm ؊1

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Section: ؊1mentioning

confidence: 68%

Spectroscopic and Electrochemical Studies on Active-site Transitions of the Type 1 Copper Protein Pseudoazurin from Achromobacter cycloclastes

Kohzuma

Dennison

McFarlane

et al. 1995

Journal of Biological Chemistry

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“…The blue single-Cu proteins whose crystal structures have been published are poplar plastocyanin (Guss & Freeman, 1983;Guss et al, 1992), Enteromorpha prolifera plastocyanin (Collyer et al, 1990), Chlamydomonas reinhardtii plastocyanin (Redinbo et al, 1993), Alcaligenes denitrificans azurin (Baler, 1988), Pseudomonas aeruginosa azurin (Adman & Jensen, 1981;Nar et al, 1991), Alcaligenes faecalis S-6 pseudoazurin (Petratos et al, 1988;Adman et al, 1989), Methylobacterium extorquens AM1 pseudoazurin (Inoue et al, 1994), Paracoccus denitrificans amicyanin (Durley et al, 1993), Thiobacillus versutus amicyanin (Romero et al, 1994), and the cucumber basic blue protein (Guss et al, 1988). The cited references deal with the structures of the proteins in the Cu II state.…”

Section: Recent Advances In the Study Of ''Blue'' Single-cu Proteinsmentioning

confidence: 97%

The Structure of a Phytocyanin, the Basic Blue Protein from Cucumber, Refined at 1.8 Å Resolution

Guss

Merritt

Phizackerley

et al. 1996

Journal of Molecular Biology

119

141

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“…X-ray crystallography has revealed that the copper ion is coordinated by His40, Cys78, His81 and Met86 (Fig. 1) [10,42,43,44,45,46]. Among these studies, the crystal structure of Achromobacter cycloclastes pseudoazurin in both oxidation states has been recently reported to high resolution [46].…”

Section: Introductionmentioning

confidence: 97%

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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Refined crystal structure of pseudoazurin from Methylobacterium extorquens AM1 at 1.5 Å resolution

Cited by 34 publications

References 5 publications

Spectroscopic and Electrochemical Studies on Active-site Transitions of the Type 1 Copper Protein Pseudoazurin from Achromobacter cycloclastes

Spectroscopic and Electrochemical Studies on Active-site Transitions of the Type 1 Copper Protein Pseudoazurin from Achromobacter cycloclastes

The Structure of a Phytocyanin, the Basic Blue Protein from Cucumber, Refined at 1.8 Å Resolution

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

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