scholarly journals The autoreducible cytochromes c of the methylotrophs Methylophilus methylotrophus and Pseudomonas AM1

1982 ◽  
Vol 207 (1) ◽  
pp. 161-165 ◽  
Author(s):  
M Beardmore-Gray ◽  
D T O'Keeffe ◽  
C Anthony
Keyword(s):  
Cytochrome C ◽  
Strong Field ◽  
The Other ◽  
Thiol Groups ◽  
High Ph ◽  
Axial Ligands ◽  
Cytochromes C ◽  
Cytochrome Cl ◽  
Haem Iron ◽  
Rule Out

The two types of soluble cytochrome c (cytochrome cH and cytochrome cL) found in methylotrophs are completely distinct proteins; one type is not a dimer or degradation product of the other. Free thiol groups are probably not involved in the unusually rapid autoreduction of the cytochromes at high pH. The axial ligands to the haem iron, histidine and methionine, are the same as in other low-spin cytochromes c. The methionine ligand is displaced at high pH by an alternative strong-field ligand. This displacement does not occur on reduction of cytochrome cL by methanol dehydrogenase, but this does not rule out the possibility that the autoreduction mechanism is involved in the interaction of the dehydrogenase and cytochrome c.

scholarly journals The interaction between methanol dehydrogenase and the autoreducible cytochromes c of the facultative methylotroph Pseudomonas AM1

1980 ◽  
Vol 190 (2) ◽  
pp. 481-484 ◽  
Author(s):  
D T O'Keeffe ◽  
C Anthony
Keyword(s):  
Cytochrome C ◽  
Methanol Dehydrogenase ◽  
High Ph ◽  
First Order ◽  
Facultative Methylotroph ◽  
Cytochromes C ◽  
Pure Methanol

Cytochromes cH and cL were autoreduced at high pH (pK greater than 10) and the autoreduced cytochromes reacted with CO. The autoreduction was first-order with respect to oxidized cytochrome c and was reversible by lowering the pH. Pure methanol dehydrogenase reduced cytochrome c (in the absence of methanol) by lowering the pK for autoreduction to less than 8.5. A mechanism is proposed for the autoreduction of cytochrome c and its involvement in the reaction with methanol dehydrogenase.

scholarly journals Effects of mutating Asn-52 to isoleucine on the haem-linked properties of cytochrome c

1994 ◽  
Vol 302 (1) ◽  
pp. 95-101 ◽  
Author(s):  
A Schejter ◽  
T I Koshy ◽  
T L Luntz ◽  
R Sanishvili ◽  
I Vig ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Site Directed Mutagenesis ◽  
Wild Type ◽  
General Increase ◽  
Reduction Potentials ◽  
Cytochromes C ◽  
In The Wild ◽  
Order Of Magnitude ◽  
The Stability ◽  
Haem Iron

Asn-52 of rat cytochrome c and baker's yeast iso-1-cytochrome c was changed to isoleucine by site-directed mutagenesis and the mutated proteins expressed in and purified from cultures of transformed yeast. This mutation affected the affinity of the haem iron for the Met-80 sulphur in the ferric state and the reduction potential of the molecule. The yeast protein, in which the sulphur-iron bond is distinctly weaker than in vertebrate cytochromes c, became very similar to the latter: the pKa of the alkaline ionization rose from 8.3 to 9.4 and that of the acidic ionization decreased from 3.4 to 2.8. The rates of binding and dissociation of cyanide became markedly lower, and the affinity was lowered by half an order of magnitude. In the ferrous state the dissociation of cyanide from the variant yeast cytochrome c was three times slower than in the wild-type. The same mutation had analogous but less pronounced effects on rat cytochrome c: it did not alter the alkaline ionization pKa nor its affinity for cyanide, but it lowered its acidic ionization pKa from 2.8 to 2.2. These results indicate that the mutation of Asn-52 to isoleucine increases the stability of the cytochrome c closed-haem crevice as observed earlier for the mutation of Tyr-67 to phenylalanine [Luntz, Schejter, Garber and Margoliash (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 3524-3528], because of either its effects on the hydrogen-bonding of an interior water molecule or a general increase in the hydrophobicity of the protein in the domain occupied by the mutated residues. The reduction potentials were affected in different ways; the Eo of rat cytochrome c rose by 14 mV whereas that of the yeast iso-1 cychrome c was 30 mV lower as a result of the change of Asn-52 to isoleucine.

scholarly journals Variation of the axial haem ligands and haem-binding motif as a probe of the Escherichia coli c-type cytochrome maturation (Ccm) system

2003 ◽  
Vol 375 (3) ◽  
pp. 721-728 ◽  
Author(s):  
James W. A. ALLEN ◽  
Stuart J. FERGUSON
Keyword(s):  
Escherichia Coli ◽  
Cytochrome C ◽  
Covalent Attachment ◽  
Binding Motif ◽  
Cytochrome C Maturation ◽  
Cytochromes C ◽  
Cytochrome C552 ◽  
Haem Iron ◽  
Made In ◽  
Uncatalysed Reaction

Cytochromes c are typically characterized by the covalent attachment of haem to polypeptide through two thioether bonds with the cysteine residues of a Cys-Xaa-Xaa-Cys-His peptide motif. In many Gram-negative bacteria, the haem is attached to the polypeptide by the periplasmically functioning cytochrome c maturation (Ccm) proteins. Exceptionally, Hydrogenobacter thermophilus cytochrome c552 can be expressed as a stable holocytochrome both in the cytoplasm of Escherichia coli in an apparently uncatalysed reaction and also in the periplasm in a Ccm-mediated reaction. In the present study we show that a Met60→Ala variant of c552, which does not have the usual distal methionine ligand to the haem iron of the mature cytochrome, can be made in the periplasm by the Ccm system. However, no holocytochrome could be detected when this variant was expressed cytoplasmically. These data highlight differences between the two modes of cytochrome c assembly. In addition, we report investigations of haem attachment to cytochromes altered to have the special Cys-Trp-Ser-Cys-Lys haem-binding motif, and Cys-Trp-Ser-Cys-His and Cys-Trp-Ala-Cys-His analogues, of the active-site haem of nitrite reductase NrfA.

scholarly journals The amino acid sequence of cytochrome c from Nigella damascena L. (love-in-a-mist)

1973 ◽  
Vol 133 (2) ◽  
pp. 251-254 ◽  
Author(s):  
R. H. Brown ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Science And Technology ◽  
The Other ◽  
Carboxypeptidase A ◽  
Cytochromes C ◽  
Lending Library ◽  
Nigella Damascena

The amino acid sequence of cytochrome c from Nigella damascena L. was determined on 0.2μmol of protein. Peptides from a single chymotryptic digest were analysed by the dansyl–Edman procedure. These peptides were ordered by reference to the sequences of other plant cytochromes c, assuming that the Nigella cytochrome is homologous with the other cytochromes. Many of the Nigella peptides were one or two residues short when compared with the corresponding chymotryptic peptides from other plant cytochromes c. These residues are assumed to have been removed by an endogenous carboxypeptidase, and the identification and placing of these residues is entirely based on homology. These residues are numbered 3, 18, 42, 43, 44, 54, 67, 72, 73, 82 and 105. A number of other positions are almost entirely placed by homology. These are positions which could not be placed definitely by dansyl–Edman analysis or by dansylation after digestion with carboxypeptidase A, and are numbered 14, 15, 16, 39, 40, 85, 86, 87 and 88. Except for residue 15, all residues based entirely, or nearly so, on homology have been previously found invariant in sequences of plant cytochromes c. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50017, at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.

scholarly journals The soluble cytochromes c of methanol-grown Hyphomicrobium X. Evidence against the involvement of autoreduction in electron-acceptor functioning of cytochrome cL

1988 ◽  
Vol 251 (2) ◽  
pp. 467-474 ◽  
Author(s):  
M Dijkstra ◽  
J Frank ◽  
J E van Wielink ◽  
J A Duine
Keyword(s):  
Electron Acceptor ◽  
Protein Molecule ◽  
Methanol Dehydrogenase ◽  
Methylotrophic Bacteria ◽  
High Ph ◽  
Native Proteins ◽  
Cytochromes C ◽  
Reverse Situation ◽  
Cytochrome Cl ◽  
Reduced Forms

Hyphomicrobium X, grown on methanol with O2 or nitrate as electron acceptor, contains two major soluble cytochromes c. These were isolated in electrophoretically homogeneous form. They are related to cytochromes c already described for other methylotrophic bacteria and designated cytochromes cH and cL (properties indicated in that order) in view of the following characteristics: absorption maxima of the reduced forms (414, 520 and 551 nm and 414, 520 and 550 nm); molar absorption coefficients of the alpha-bands (23,700 M-1.cm-1 and 21,600 M-1.cm-1); maxima of the alpha-bands (no splitting) at 77 K (547.6 nm and 548.5 nm); Mr values of the native proteins (15,000 and 19,500); pI values (7.4 and 7.5, and 4.3); midpoint potentials at pH 7.0 (+292 mV and +270 mV). Both were monomers containing 1 haem c group per protein molecule, the oxidized forms binding cyanide at high pH. Autoreduction also occurred at high pH but at a rate significantly lower than that reported for other ferricytochromes c. On the other hand, the reverse situation applies to the reduction of ferricytochrome cL by reduced methanol dehydrogenase, the reduction occurring instantaneously at pH 7 but much more slowly at pH 9 (ferricytochrome cH was reduced at a 7-fold lower rate, but the rates at pH 7 and 9 were similar). Insignificant reduction was observed with cyclopropanol-inactivated enzyme or with enzyme in the presence of EDTA. In view of the dissimilarities, it is concluded that different mechanisms operate in the autoreduction of ferricytochrome cL and in its reduction by reduced methanol dehydrogenase.

scholarly journals Structural role of the tyrosine residues of cytochrome c

1982 ◽  
Vol 205 (1) ◽  
pp. 153-165 ◽  
Author(s):  
C G Eley ◽  
G R Moore ◽  
R J Williams ◽  
W Neupert ◽  
P J Boon ◽  
...  
Keyword(s):  
Amino Acid ◽  
High Resolution ◽  
Cytochrome C ◽  
Amino Acid Sequences ◽  
The Other ◽  
Amino Acid Substitutions ◽  
Tertiary Structures ◽  
Tyrosine Residues ◽  
Cytochromes C

The tertiary structures of horse, tuna, Neurospora crassa, horse [Hse65,Leu67]- and horse [Hse65,Leu74]-cytochromes c were studied with high-resolution 1H n.m.r. spectroscopy. The amino acid sequences of these proteins differ at position 46, which is occupied by phenylalanine in the horse proteins but by tyrosine in the remaining two, and at positions 67, 74 and 97, which are all occupied by tyrosine residues in horse and tuna cytochrome c but in the other proteins are substituted by phenylalanine or leucine, though there is only one such substitution per protein. The various aromatic-amino-acid substitutions do not seriously affect the protein structure.

scholarly journals The comparative structure of mammalian glyceraldehyde 3-phosphate dehydrogenase

1969 ◽  
Vol 111 (1) ◽  
pp. 17-21 ◽  
Author(s):  
R N Perham
Keyword(s):  
Amino Acid ◽  
Essential Role ◽  
Polypeptide Chain ◽  
Thiol Group ◽  
Preliminary Evidence ◽  
Amino Acid Sequences ◽  
The Other ◽  
Thiol Groups ◽  
Comparative Structure ◽  
Rule Out

1. The amino acid sequences around the thiol groups of glyceraldehyde 3-phosphate dehydrogenase from badger and monkey skeletal muscle were compared with the sequences around the thiol groups in the enzyme isolated from other organisms. 2. Preliminary evidence of the existence of isoenzymes in the badger was obtained. Only the major form, however, could be purified completely. 3. The monkey enzyme contains only three cysteine residues per polypeptide chain compared with the four found in all the other mammalian enzymes so far examined, including that of badger, and the two in yeast. The missing thiol group in monkey was identified as residue 281 in the corresponding sequence of the pig enzyme. 4. These experiments rule out any essential role for cysteine-281 in the function of the mammalian enzymes. 5. Further evidence of the remarkable conservation of amino acid sequence in this enzyme during evolution is presented and discussed.

THE AMINO ACID SEQUENCE OF CYTOCHROMEcIN RELATION TO ITS FUNCTION AND EVOLUTION

1964 ◽  
Vol 42 (6) ◽  
pp. 745-753 ◽  
Author(s):  
E. Margoliash
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
The Other ◽  
Functional Activities ◽  
Cytochromes C ◽  
The One ◽  
Structural Aspects

A comparison of the amino acid sequences of the cytochromes c from horse, pig, rabbit, chicken, and man leads to the conclusion that all have derived phylogenetically from a common primordial cytochrome c. The significance of the constant and of the variable features of these sequences with regard, on the one hand, to the structural aspects of the functional activities of the protein, and on the other, to the evolutionary relations between the various cytochromes c is discussed.

Modernism, Empiricism, and Rationalism

2016 ◽  
Vol 46 (1) ◽  
pp. 38-47
Author(s):  
Geoffrey Squires
Keyword(s):  
Twentieth Century ◽  
The Other ◽  
Modern Poetry ◽  
Philosophical Perspective ◽  
Irish Poetry ◽  
Dimensional Spectrum ◽  
Culture History ◽  
The World ◽  
The Impact ◽  
Rule Out

Modernism is usually defined historically as the composite movement at the beginning of the twentieth century which led to a radical break with what had gone before in literature and the other arts. Given the problems of the continuing use of the concept to cover subsequent writing, this essay proposes an alternative, philosophical perspective which explores the impact of rationalism (what we bring to the world) on the prevailing empiricism (what we take from the world) of modern poetry, which leads to a concern with consciousness rather than experience. This in turn involves a re-conceptualisation of the lyric or narrative I, of language itself as a phenomenon, and of other poetic themes such as nature, culture, history, and art. Against the background of the dominant empiricism of modern Irish poetry as presented in Crotty's anthology, the essay explores these ideas in terms of a small number of poets who may be considered modernist in various ways. This does not rule out modernist elements in some other poets and the initial distinction between a poetics of experience and one of consciousness is better seen as a multi-dimensional spectrum that requires further, more detailed analysis than is possible here.

Modeling and risk analysis of bromate formation from ozonation of bromide-containing waters

1996 ◽  
Vol 34 (7-8) ◽  
pp. 79-85 ◽  
Author(s):  
Rengao Song ◽  
Roger Minear ◽  
Paul Westerhoff ◽  
Gary Amy
Keyword(s):  
Water Quality ◽  
Risk Analysis ◽  
Ammonia Concentration ◽  
Quality Characteristics ◽  
The Other ◽  
High Ph ◽  
Treatment Processes ◽  
Ozone Dose ◽  
Other Hand

Empirical bromate formation models were developed from batch ozonation data to simulate the effects of important water quality characteristics and treatment processes on bromate formation. Bromate formation was favored at high pH, bromide concentration, alkalinity, and ozone dose. On the other hand, increasing DOC and ammonia concentration decreased bromate formation. Validation of the bromate models demonstrated that the models accurately simulated bromate formation. Risk analysis of bromate formation was performed on 5 utilities in which ozone was used, and it was concluded that under typical ozonation conditions, the associated risk related to bromate formation could be as high as 10−3.

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