The P450camG248E Mutant Covalently Binds Its Prosthetic Heme Group†

Biochemistry ◽  
2005 ◽  
Vol 44 (10) ◽  
pp. 4091-4099 ◽  
Author(s):  
Julian Limburg ◽  
Laurie A. LeBrun ◽  
Paul R. Ortiz de Montellano
Keyword(s):  
Heme Group ◽  
Prosthetic Heme Group

Dioxygenation of Human Serum Albumin Having a Prosthetic Heme Group in a Tailor-Made Heme Pocket

2004 ◽  
Vol 126 (44) ◽  
pp. 14304-14305 ◽  
Author(s):  
Teruyuki Komatsu ◽  
Naomi Ohmichi ◽  
Patricia A. Zunszain ◽  
Stephen Curry ◽  
Eishun Tsuchida
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Heme Group ◽  
Heme Pocket ◽  
Prosthetic Heme Group

scholarly journals Asp-225 and Glu-375 in Autocatalytic Attachment of the Prosthetic Heme Group of Lactoperoxidase

2001 ◽  
Vol 277 (9) ◽  
pp. 7191-7200 ◽  
Author(s):  
Christophe Colas ◽  
Jane M. Kuo ◽  
Paul R. Ortiz de Montellano
Keyword(s):  
Heme Group ◽  
Prosthetic Heme Group

scholarly journals Sedimentary Cobalt Protoporphyrin as a Potential Precursor of Prosthetic Heme Group for Bacteria Inhabiting Fossil Organic Matter-Rich Shale Rock

Biomolecules ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1913
Author(s):  
Robert Stasiuk ◽  
Renata Matlakowska
Keyword(s):  
Bacterial Culture ◽  
Heme Iron ◽  
Heme Biosynthesis ◽  
Bacterial Cells ◽  
Heme Group ◽  
Qualitative And Quantitative ◽  
Shale Rock ◽  
Cobalt Protoporphyrin ◽  
Prosthetic Heme Group ◽  
Potential Precursor

This study hypothesizes that bacteria inhabiting shale rock affect the content of the sedimentary cobalt protoporphyrin present in it and can use it as a precursor for heme synthesis. To verify this hypothesis, we conducted qualitative and quantitative comparative analyses of cobalt protoporphyrin as well as heme, and heme iron in shale rock that were (i) inhabited by bacteria in the field, (ii) treated with bacteria in the laboratory, and with (iii) bacterial culture on synthetic cobalt protoporphyrin. Additionally, we examined the above-mentioned samples for the presence of enzymes involved in the heme biosynthesis and uptake as well as hemoproteins. We found depletion of cobalt protoporphyrin and a much higher heme concentration in the shale rock inhabited by bacteria in the field as well as the shale rock treated with bacteria in the laboratory. Similarly, we observed the accumulation of protoporphyrin in bacterial cells grown on synthetic cobalt protoporphyrin. We detected numerous hemoproteins in metaproteome of bacteria inhabited shale rock in the field and in proteomes of bacteria inhabited shale rock and synthetic cobalt protoporhyrin in the laboratory, but none of them had all the enzymes involved in the heme biosynthesis. However, proteins responsible for heme uptake, ferrochelatase and sirohydrochlorin cobaltochelatase/sirohydrochlorin cobalt-lyase were detected in all studied samples.

scholarly journals Histolysis, Histogenesis, and Differentiation during Insect Metamorphosis in Relation to Metabolic Changes

Development ◽  
1953 ◽  
Vol 1 (3) ◽  
pp. 279-282
Author(s):  
Ivar Agrell
Keyword(s):  
Oxygen Consumption ◽  
Metabolic Activity ◽  
Marked Decrease ◽  
Metabolic Changes ◽  
Limiting Factor ◽  
Heme Group ◽  
Enzyme Systems ◽  
Insect Metamorphosis ◽  
Prosthetic Heme Group ◽  
Protein Part

The most obvious change in metabolism during the more advanced type of insect metamorphosis is the change in the integral metabolic activity. After pupation there is first a marked decrease and later an increase of, for instance, the oxygen consumption. The respiratory metabolic curve is U-shaped. The cause of this change is a corresponding variation in the activity of oxidative enzyme systems. If one compares the variation of the spontaneous Mb-reduction and of the oxygen consumption in the fly Calliphora, one finds that the two curves have almost the same course (Agrell, 1947b). This shows an important co-operation of the dehydrogenase systems. The cytochrome system also shows a similar U-shaped variation during the period of metamorphosis, according to Wolsky (1938), Williams (1948) and Sacktor (1950). One limiting factor is the protein part of the enzymes, which is first broken down and later rebuilt (Agrell, 1946). Another limiting factor is the prosthetic heme group in the cytochromes (Williams, 1951).

scholarly journals Horseradish Peroxidase Mutants That Autocatalytically Modify Their Prosthetic Heme Group

2004 ◽  
Vol 279 (23) ◽  
pp. 24131-24140 ◽  
Author(s):  
Christophe Colas ◽  
Paul R. Ortiz de Montellano
Keyword(s):  
Horseradish Peroxidase ◽  
Heme Group ◽  
Prosthetic Heme Group

scholarly journals Conformational changes in myeloperoxidase induced by ubiquitin and NETs containing free ISG15 from systemic lupus erythematosus patients promote a pro-inflammatory cytokine response in CD4+ T cells

2020 ◽  
Vol 18 (1) ◽  
Author(s):  
Daniel Alberto Carrillo-Vázquez ◽  
Eduardo Jardón-Valadez ◽  
Jiram Torres-Ruiz ◽  
Guillermo Juárez-Vega ◽  
José Luis Maravillas-Montero ◽  
...  
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Molecular Dynamics ◽  
Conformational Changes ◽  
Lupus Erythematosus ◽  
Structural Changes ◽  
Hydration Status ◽  
Healthy Controls ◽  
Heme Group ◽  
Systemic Lupus ◽  
The Impact

Abstract Background Neutrophil extracellular traps (NETs) from patients with systemic lupus erythematosus (SLE) are characterized by lower ubiquitylation and myeloperoxidase (MPO) as a substrate. The structural and functional effect of such modification and if there are additional post-translational modifications (PTMs) are unknown. Methods To assess the expression and functional role of PTMs in NETs of patients with SLE; reactivation, proliferation and cytokine production was evaluated by flow cytometry using co-cultures with dendritic cells (DC) and CD4+ from SLE patients and healthy controls. The impact of ubiquitylation on MPO was assessed by molecular dynamics. The expression of ISG15 in NETs was evaluated by immunofluorescence and Western Blot. Results Fifteen patients with SLE and ten healthy controls were included. In the co-cultures of CD4+ lymphocytes with DC stimulated with ubiquitylated MPO or recombinant MPO, a higher expression of IFNγ and IL-17A was found in CD4+ from SLE patients (p < 0.05). Furthermore, with DC stimulated with ubiquitylated MPO a trend towards increased expression of CD25 and Ki67 was found in lupus CD4+ lymphocytes, while the opposite was documented in controls (p < 0.05). Through molecular dynamics we found the K129-K488-K505 residues of MPO as susceptible to ubiquitylation. Ubiquitylation affects the hydration status of the HEME group depending on the residue to which it is conjugated. R239 was found near by the HEME group when the ubiquitin was in K488-K505. In addition, we found greater expression of ISG15 in the SLE NETs vs controls (p < 0.05), colocalization with H2B (r = 0.81) only in SLE samples and increased production of IFNγ in PBMCs stimulated with lupus NETs compared to healthy controls NETs. Conclusion The ubiquitylated MPO has a differential effect on the induction of reactivation of CD4+ lymphocytes in patients with SLE, which may be related to structural changes by ubiquitylation at the catalytic site of MPO. Besides a lower ubiquitylation pattern, NETs of patients with SLE are characterized by the expression of ISG15, and the induction of IFNγ by Th1 cells.

Interaction between pyridine nucleotide coenzymes and heme proteins as a possible source of error in assay of activities of coenzyme-linked enzyme.

1989 ◽  
Vol 35 (10) ◽  
pp. 2129-2133 ◽  
Author(s):  
M D Jeyasingham ◽  
O E Pratt ◽  
H K Roopral
Keyword(s):  
Pyridine Nucleotide ◽  
Peak Height ◽  
Heme Group ◽  
Ultraviolet Absorbance ◽  
The Third ◽  
Spectral Shifts ◽  
Muscle Breakdown ◽  
Activity Of Enzymes ◽  
Source Of Error ◽  
Absorbance Spectra

Abstract The ultraviolet absorbance spectra of pyridine nucleotide coenzymes change in the presence of heme-containing proteins. The positions of each of the two main absorbance peaks of NADH are shifted progressively towards shorter wavelengths in the presence of increasing concentrations of hemoglobin, and the third peak, at 220 nm, disappears altogether. Similar changes are seen in the spectra of NAD+ and NADPH, and similar effects on these spectra are produced by myoglobin and cytochrome c, but not by comparable concentrations of albumin. The spectral shifts are generally accompanied by a decreased peak height. This finding may help explain problems reported by previous workers in the measurement of the activity of enzymes such as transketolase or lactate dehydrogenase in erythrocyte hemolysates. Errors may be considerable if allowance is not made for this effect, especially if the concentration of heme protein in the spectrophotometer cuvette much exceeds 1 g/L. The interaction appears to indicate some form of bonding, occurring generally between pyridine nucleotide coenzymes and the heme group in proteins. We relate the findings to measurement of activities of pyridine nucleotide-linked enzymes in erythrocyte lysates and in plasma containing myoglobin after muscle breakdown.

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