Sequential proton NMR assignments of iron(II) cytochrome c551 from Pseudomonas aeruginosa

Detlefsen, David J.; Thanabal, V.; Pecoraro, V.L.; Wagner, Gerhard

doi:10.1021/bi00492a011

Cited by 20 publications

(23 citation statements)

References 40 publications

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“…The rmsd of main chain atoms (N, CR, C′) of residues 1-78 (HT c-552 numbering) is 1.00 Å between these two structures. This value is comparable to the rmsd value of 1.23 Å between the crystal structure of PA c-551 and NMR solution structures of PS c-551 and PZ c-551 (28,29) and smaller than the average rmsd of 1.90 Å between the crystal and ten NMR solution structures of PA c-551 (12). Notwithstanding the similarity between the main chain foldings of HT c-552 and PA c-551, the former is more stable to heat than the latter (6).…”

Section: Discussionsupporting

confidence: 56%

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Solution Structure of Thermostable Cytochrome c-552 from Hydrogenobacter thermophilus Determined by ¹H-NMR Spectroscopy^,

et al. 1998

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The solution structure of a thermostable cytochrome c-552 from a thermophilic hydrogen oxidizing bacterium Hydrogenobacter thermophilus was determined by proton nuclear magnetic resonance spectroscopy. Twenty structures were calculated by the X-PLOR program on the basis of 902 interproton distances, 21 hydrogen bonds, and 13 torsion angle constraints. The pairwise average root-mean-square deviation for the main chain heavy atoms was 0.91 +/- 0.11 A. The main chain folding of the cytochrome c-552 was almost the same as that of Pseudomonas aeruginosa cytochrome c-551 that has 59% sequence identity to the cytochrome c-552 but is less thermostable. We found several differences in local structures between the cytochromes c-552 and c-551. In the cytochrome c-552, aromatic-amino interactions were uniquely formed between Arg 35 and Tyr 32 and/or Tyr 41, the latter also having hydrophobic contacts with the side chains of Tyr 32, Ala 38, and Leu 42. Small hydrophobic cores were more tightly packed in the cytochrome c-552 because of the occupancies of Ala 5, Met 11, and Ile 76, each substituted by Phe 7, Val 13, and Val 78, respectively, in the cytochrome c-551. Some of these structural differences may contribute to the higher thermostability of the cytochrome c-552.

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Section: Discussionsupporting

confidence: 56%

“…e The PROCHECK-NMR program (45) was used to assess the stereochemical parameters of the family of conformers. results were obtained in the exchange experiment of PA c-551 analyzed by 1 H NMR (12).…”

Section: Resultsmentioning

confidence: 99%

Solution Structure of Thermostable Cytochrome c-552 from Hydrogenobacter thermophilus Determined by ¹H-NMR Spectroscopy^,

et al. 1998

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“…Heme assignment. The heme protons were assigned according to a procedure originally described by Keller and Wiithrich (1978) (see also Detlefsen et al, 1990). "C assignments were obtained from the HSQC experiment.…”

Section: Resultsmentioning

confidence: 99%

¹H and ¹³C NMR Assignments and Structural Aspects of a Ferrocytochrome c‐551 from the Purple Phototrophic Bacterium Ectothiorhodospira halophila

Bersch¹,

Brutscher²,

Meyer³

et al. 1995

European Journal of Biochemistry

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Two-dimensional nuclear magnetic resonance was used to assign the 'H and I3C resonances of ferrocytochrome c-551 from Ectothiorhodospira halophila, a halophilic phototrophic purple bacterium. This 78-residue protein belongs to a small subgroup of class I cytochromes c together with the analogous cytochromes c-551 from E. halochloris and E. abdelmalekii. A nearly complete assignment of 13C resonances was obtained at natural abundance using a gradient-enhanced 'H-detected heteronuclear single quantum coherence experiment (HSQC). This was found to be extremely useful for the unambigous assignment of side chain protons. The secondary structure of the protein was determined from analyses of short-and medium-range nuclear Overhauser enhancements (NOE), amide proton exchange and I3Ca chemical shifts. Three helices could be identified which are well conserved among the class I cytochromes c. There is some evidence for two other regions of less well defined helical structure. From a preliminary analysis of long-range NOE it is shown that in the E. halophila cytochrome c-551 the general cytochrome c fold is well conserved, including the three conserved helices (residues 2-8, 41 -50, 63-76), the regions around the heme ligands (Cysl4-Serl5-Serl6-Cys17-His18, Met55) and the SZ loop (residues 18-28). In addition, three variable segments of the protein are discussed in detail, one of those including a cisproline, a feature so far unique in the cytochrome c family. Structural alignments of the E. halophila cytochrome c-551 with two other Pseudomonas cytochrome c5 homologs (Azotobacter vinelandii cytochrome c5 and Chlorobium limicola cytochrome c-555) are provided which are based on sequence similarities and secondary structure alignments.

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“…Assignments for 1 H NMR chemical shifts were made according to standard procedures (35). Measurements of chemical shifts for reduced Pa Cyt c 551 were guided by published assignments (36)(37)(38). Heme methyl shifts for Ht Cyt c 552 at 323 K were determined by a 1D variable-temperature NMR experiment (300-344 K).…”

Section: Methodsmentioning

confidence: 99%

Heme axial methionine fluxionality in Hydrogenobacter thermophilus cytochrome c ₅₅₂

Zhong

Wen

Rabinowitz

et al. 2004

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

122

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The heme group in paramagnetic (S ‫؍‬ 1͞2) ferricytochromes c typically displays a markedly asymmetric distribution of unpaired electron spin density among the heme pyrrole ␤ substituents. This asymmetry is determined by the orientations of the heme axial ligands, histidine and methionine. One exception to this is ferricytochrome c552 from Hydrogenobacter thermophilus, which has similar amounts of unpaired electron spin density at the ␤ substituents on all four heme pyrroles. Here, determination of the orientation of the magnetic axes and analysis of NMR line shapes for H. thermophilus ferricytochrome c 552 is performed. These data reveal that the unusual electronic structure for this protein is a result of fluxionality of the heme axial methionine. It is proposed that the ligand undergoes inversion at the pyramidal sulfur, and the rapid interconversion between two diastereomeric forms results in the unusual heme electronic structure. Thus a fluxional process for a metal-bound amino acid side chain has now been identified.

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Sequential proton NMR assignments of iron(II) cytochrome c551 from Pseudomonas aeruginosa

Cited by 20 publications

References 40 publications

Solution Structure of Thermostable Cytochrome c-552 from Hydrogenobacter thermophilus Determined by ¹H-NMR Spectroscopy^,

Solution Structure of Thermostable Cytochrome c-552 from Hydrogenobacter thermophilus Determined by ¹H-NMR Spectroscopy^,

¹H and ¹³C NMR Assignments and Structural Aspects of a Ferrocytochrome c‐551 from the Purple Phototrophic Bacterium Ectothiorhodospira halophila

Heme axial methionine fluxionality in Hydrogenobacter thermophilus cytochrome c ₅₅₂

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Sequential proton NMR assignments of iron(II) cytochrome c551 from Pseudomonas aeruginosa

Cited by 20 publications

References 40 publications

Solution Structure of Thermostable Cytochrome c-552 from Hydrogenobacter thermophilus Determined by 1H-NMR Spectroscopy,

Solution Structure of Thermostable Cytochrome c-552 from Hydrogenobacter thermophilus Determined by 1H-NMR Spectroscopy,

1H and 13C NMR Assignments and Structural Aspects of a Ferrocytochrome c‐551 from the Purple Phototrophic Bacterium Ectothiorhodospira halophila

Heme axial methionine fluxionality in Hydrogenobacter thermophilus cytochrome c 552

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Solution Structure of Thermostable Cytochrome c-552 from Hydrogenobacter thermophilus Determined by ¹H-NMR Spectroscopy^,

Solution Structure of Thermostable Cytochrome c-552 from Hydrogenobacter thermophilus Determined by ¹H-NMR Spectroscopy^,

¹H and ¹³C NMR Assignments and Structural Aspects of a Ferrocytochrome c‐551 from the Purple Phototrophic Bacterium Ectothiorhodospira halophila

Heme axial methionine fluxionality in Hydrogenobacter thermophilus cytochrome c ₅₅₂