Insight into Heme Protein Redox Potential Control and Functional Aspects of Six-Coordinate Ligand-Sensing Heme Proteins from Studies of Synthetic Heme Peptides

2006 ◽  
Vol 45 (25) ◽  
pp. 9985-10001 ◽  
Author(s):  
Aaron B. Cowley ◽  
Michelle L. Kennedy ◽  
Svetlana Silchenko ◽  
Gudrun S. Lukat-Rodgers ◽  
Kenton R. Rodgers ◽  
...  
Keyword(s):  
Redox Potential ◽  
Heme Proteins ◽  
Heme Protein ◽  
Potential Control ◽  
Functional Aspects ◽  
Heme Peptides ◽  
Insight Into

scholarly journals Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide pKa: Insight into Axial Ligand Tuning in Heme Protein Catalysis

2014 ◽  
Vol 136 (25) ◽  
pp. 9124-9131 ◽  
Author(s):  
Timothy H. Yosca ◽  
Rachel K. Behan ◽  
Courtney M. Krest ◽  
Elizabeth L. Onderko ◽  
Matthew C. Langston ◽  
...  
Keyword(s):  
Heme Protein ◽  
Axial Ligand ◽  
Upper Limit ◽  
Insight Into ◽  
Protein Catalysis

scholarly journals Annotation and Expression of IDN2-like and FDM-like Genes in Sexual and Aposporous Hypericum perforatum L. accessions

Plants ◽  
2019 ◽  
Vol 8 (6) ◽  
pp. 158
Author(s):  
Andrea Basso ◽  
Gianni Barcaccia ◽  
Giulio Galla
Keyword(s):  
Cell Fate ◽  
Hypericum Perforatum ◽  
Seed Set ◽  
Regulation Of Gene Expression ◽  
Cell Fate Determination ◽  
Functional Aspects ◽  
Hypericum Perforatum L ◽  
Potential Interactions ◽  
Insight Into ◽  
Reproductive Phenotype

The protein IDN2, together with the highly similar interactors FDM1 and FDM2, is required for RNA-directed DNA methylation (RdDM) and siRNA production. Epigenetic regulation of gene expression is required to restrict cell fate determination in A. thaliana ovules. Recently, three transcripts sharing high similarity with the A. thaliana IDN2 and FDM1-2 were found to be differentially expressed in ovules of apomictic Hypericum perforatum L. accessions. To gain further insight into the expression and regulation of these genes in the context of apomixis, we investigated genomic, transcriptional and functional aspects of the gene family in this species. The H. perforatum genome encodes for two IDN2-like and 7 FDM-like genes. Differential and heterochronic expression of FDM4-like genes was found in H. perforatum pistils. The involvement of these genes in reproduction and seed development is consistent with the observed reduction of the seed set and high variability in seed size in A. thaliana IDN2 and FDM-like knockout lines. Differential expression of IDN2-like and FDM-like genes in H. perforatum was predicted to affect the network of potential interactions between these proteins. Furthermore, pistil transcript levels are modulated by cytokinin and auxin but the effect operated by the two hormones depends on the reproductive phenotype.

Heme protein biosensors

2000 ◽  
Vol 04 (04) ◽  
pp. 358-361 ◽  
Author(s):  
MICHAEL K. CHAN
Keyword(s):  
Nitric Oxide ◽  
Structure Function ◽  
Guanylate Cyclase ◽  
Heme Proteins ◽  
Rhodospirillum Rubrum ◽  
Soluble Guanylate Cyclase ◽  
Heme Protein ◽  
Novel Proteins ◽  
Current State ◽  
Protein Sensors

The recent discovery that heme proteins can serve as molecular biosensors has opened up a new direction in heme biochemistry directed towards elucidating their structure-function relationships. Examples of such sensory heme proteins include the FixL proteins of Rhizobia involved in oxygen sensing, the CooA protein of Rhodospirillum rubrum that senses CO, and the mammalian soluble guanylate cyclase—the only proven nitric oxide receptor. This overview summarizes the current state of knowledge regarding the roles and mechanisms of these novel proteins and discusses the evidence for other putative heme protein sensors. These topics will be presented in the Heme Protein Biosensors Symposium at the First International Conference of Porphyrins and Phthalocyanines in Dijon, France.

scholarly journals Redox Potential Control by Drug Binding to Cytochrome P450 3A4

2007 ◽  
Vol 129 (45) ◽  
pp. 13778-13779 ◽  
Author(s):  
Aditi Das ◽  
Yelena V. Grinkova ◽  
Stephen G. Sligar
Keyword(s):  
Cytochrome P450 ◽  
Redox Potential ◽  
Drug Binding ◽  
Cytochrome P450 3A4 ◽  
Potential Control

scholarly journals Microbiological Redox Potential Control to Improve the Efficiency of Chalcopyrite Bioleaching

2018 ◽  
Vol 35 (8) ◽  
pp. 648-656 ◽  
Author(s):  
Yusei Masaki ◽  
Tsuyoshi Hirajima ◽  
Keiko Sasaki ◽  
Hajime Miki ◽  
Naoko Okibe
Keyword(s):  
Redox Potential ◽  
Potential Control

scholarly journals High affinity histamine-binding and antihistaminic activity of the salivary nitric oxide-carrying heme protein (nitrophorin) of Rhodnius prolixus.

1994 ◽  
Vol 180 (6) ◽  
pp. 2251-2257 ◽  
Author(s):  
J M Ribeiro ◽  
F A Walker
Keyword(s):  
Nitric Oxide ◽  
Heme Proteins ◽  
Soret Band ◽  
Heme Protein ◽  
Rhodnius Prolixus ◽  
Difference Spectra ◽  
The Difference ◽  
Histamine Binding ◽  
Hematophagous Arthropods ◽  
Molecular Sieving

The salivary glands of Rhodnius prolixus contain a nitrosyl-heme protein, named nitrophorin, that releases the vasodilatory and antiplatelet compound nitric oxide (NO). Because imidazole compounds such as histamine can interact with Fe(III) heme proteins, we investigated whether such substances could interact with Rhodnius nitrophorins. Both imidazole and histamine, but not histidine can produce full of the difference spectra of the Soret band in the 1-3 microM concentration range (at a heme protein concentration of 0.4 microM). The apparent K0.5 for the binding of histamine with the heme protein is below 1 microM. Furthermore, the complex histamine-heme protein does not dissociate after molecular sieving chromatography. To investigate whether histamine could displace NO from the native nitrosyl nitrophorins, histamine was added to the native heme proteins, leading to displacement of the bound NO as observed by changes in the absorption spectra as well as by the production of nitrite. Finally, the antihistamine effect of the heme protein was demonstrated by its inhibition of the histamine-provoked contractures of the guinea pig ileum. It is concluded that histamine, a common autacoid found at the site of injury and exposure to antigenic substances such as the site of feeding by hematophagous arthropods, can be scavenged by the nitrosyl nitrophorin of R. prolixus, which, in return, will release the vasodilatory and platelet inhibiting NO to counteract the host hemostatic response.

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