Hydrogen bond-linked pathways of peptide units and polar groups of amino acid residues suitable for electron transfer in cytochrome c proteins

2018 ◽  
Vol 453 (1-2) ◽  
pp. 197-203 ◽  
Author(s):  
T. Ramasarma ◽  
D. Vaigundan
Keyword(s):  
Hydrogen Bond ◽  
Electron Transfer ◽  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Residues ◽  
Polar Groups ◽  
C Proteins

scholarly journals Hydrogen Bond Strengths in Phosphorylated and Sulfated Amino Acid Residues

PLoS ONE ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. e57804 ◽  
Author(s):  
Chaya Rapp ◽  
Hadassa Klerman ◽  
Emily Levine ◽  
Christopher L. McClendon
Keyword(s):  
Hydrogen Bond ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Bond Strengths

Electron Transfer Reaction of Glucose Oxidase Hybrids Modified with PhenothiazineviaPoly(ethylene oxide) Spacer on Acidic Amino Acid Residues

2002 ◽  
Vol 31 (2) ◽  
pp. 256-257 ◽  
Author(s):  
Sayuri Aoki ◽  
Kunikazu Ishii ◽  
Takeshi Ueki ◽  
Kazumichi Ban ◽  
Shin-ichiro Imabayashi ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Amino Acid ◽  
Ethylene Oxide ◽  
Glucose Oxidase ◽  
Transfer Reaction ◽  
Electron Transfer Reaction ◽  
Amino Acid Residues ◽  
Acidic Amino Acid

scholarly journals Helix Formation in Preorganized β/γ-Peptide Foldamers: Hydrogen-Bond Analogy to the α-Helix without α-Amino Acid Residues

2010 ◽  
Vol 132 (23) ◽  
pp. 7868-7869 ◽  
Author(s):  
Li Guo ◽  
Aaron M. Almeida ◽  
Weicheng Zhang ◽  
Andrew G. Reidenbach ◽  
Soo Hyuk Choi ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Helix Formation ◽  
Α Helix

scholarly journals The amino acid sequence of sesame (Sesamum indicum L.) and castor (Ricinus communis L.) cytochrome c

1971 ◽  
Vol 121 (3) ◽  
pp. 439-446 ◽  
Author(s):  
E. W. Thompson ◽  
M. Richardson ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Mung Bean ◽  
Ricinus Communis ◽  
Sesamum Indicum ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Single Chain ◽  
Ricinus Communis L ◽  
Lysine Residues

The amino acid sequences of sesame (Sesamum indicum L.) and castor (Ricinus communis L.) cytochrome c were determined by using 1.5μmol of protein from each species. Both molecules consist of a single chain of 111 amino acid residues and are homologous with other mitochondrial cytochrome c molecules. Both have an N-acetylated ‘tail’ of eight amino acids and two ∈-N-trimethyl-lysine residues, as also reported for wheat germ (Delange, Glazer & Smith, 1969) and mung-bean cytochrome c (Thompson, Laycock, Ramshaw & Boulter, 1970). Two different preparations of castor cytochrome c differed by one residue. This was glutamic acid for glutamine in position 100. The results for sesame and castor cytochrome c led to a re-examination and subsequent correction to the N-terminal region of the mung-bean cytochrome c sequence, as given by Thompson et al. (1970).

scholarly journals Structural analyses of the deduced amino acid sequences of a novel type heme–copper terminal oxidase, cytochrome aco3, from alkalophilic Bacillus YN-2000

2001 ◽  
Vol 47 (12) ◽  
pp. 1075-1081 ◽  
Author(s):  
Kimitoshi Denda ◽  
Akira Oshima ◽  
Yoshihiro Fukumori
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Basic Amino Acid ◽  
Structural Features ◽  
Thermophilic Bacterium ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Gene Encoding ◽  
Bacterium Bacillus ◽  
Alkalophilic Bacillus

Cytochrome aco3 from a facultatively alkalophilic bacterium, Bacillus YN-2000, was found to be alkaline- and heat-tolerant. To better understand the structural features of Bacillus YN-2000 cytochrome aco3, the gene encoding this enzyme was cloned and sequenced. Nucleotide sequence analyses of the region neighboring the acoI (subunit I) gene revealed that the acoII (subunit II) and acoIII (subunit III) genes were concomitantly clustered upstream and downstream of the acoI gene, respectively, forming an operon with transcriptional polarity. The deduced amino acid sequence of subunit I was highly similar to that of cytochrome caa3 from thermophilic bacterium Bacillus PS3 in which the heme a3 could be replaced with heme o. Furthermore, a marked paucity of basic amino acid residues was found in the cytochrome c-binding subunit II, which might be a result of the adaptation to a highly alkaline external milieu.Key words: cytochrome c oxidase, alkalophile, thermostability, heme o, Bacilli.

The Amino Acid Sequence of Cytochrome c-553 from the Chrysophycean Alga Monochrysis lutheri

1972 ◽  
Vol 50 (12) ◽  
pp. 1311-1325 ◽  
Author(s):  
M. V. Laycock
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Photosynthetic Apparatus ◽  
Amino Acid Residues ◽  
Unicellular Alga ◽  
Electron Carrier ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of cytochrome c-553, an electron carrier in the photosynthetic apparatus of the unicellular alga Monochrysis lutheri, has been determined. The protein consists of a single polypeptide chain of 83 amino acid residues. The sequence shows homology with mitochondrial cytochrome c at each end of the chain. The N-terminal glycine is not acetylated and corresponds to position 1 of mammalian cytochrome c when the cysteine residues of the two proteins are aligned.

scholarly journals Proton-assisted Two-electron Transfer in Natural Variants of Tetraheme Cytochromes fromDesulfomicrobiumSp.

2004 ◽  
Vol 279 (50) ◽  
pp. 52227-52237 ◽  
Author(s):  
Ilídio J. Correia ◽  
Catarina M. Paquete ◽  
Ana Coelho ◽  
Claudia C. Almeida ◽  
Teresa Catarino ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Amino Acid ◽  
Hydrogen Uptake ◽  
Single Amino Acid ◽  
Amino Acid Residues ◽  
Tertiary Structures ◽  
X Ray Crystallography ◽  
Natural Variants ◽  
Uptake Activity ◽  
Tetraheme Cytochrome

The tetraheme cytochromec3isolated fromDesulfomicrobium baculatum(DSM 1743)(Dsmb) was cloned, and the sequence analysis showed that this cytochrome differs in just three amino acid residues from the cytochromec3isolated fromDesulfomicrobium norvegicum(Dsmn): (DsmnXXDsmb) Thr-37 → Ser, Val-45 → Ala, and Phe-88 → Tyr. X-ray crystallography was used to determine the structure of cytochromec3fromDsmb, showing that it is very similar to the published structure of cytochromec3fromDsmn. A detailed thermodynamic and kinetic characterization of these two tetraheme cytochromesc3was performed by using NMR and visible spectroscopy. The results obtained show that the network of cooperativities between the redox and protonic centers is consistent with a synergetic process to stimulate the hydrogen uptake activity of hydrogenase. This is achieved by increasing the affinity of the cytochrome for protons through binding electrons and, reciprocally, by favoring a concerted two-electron transfer assisted by the binding of proton(s). The data were analyzed within the framework of the differences in the primary and tertiary structures of the two proteins, showing that residue 88, close to heme I, is the main cause for the differences in the microscopic thermodynamic parameters obtained for these two cytochromesc3. This comparison reveals how replacement of a single amino acid can tune the functional properties of energy-transducing proteins, so that they can be optimized to suit the bioenergetic constraints of specific habitats.

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