Reactions of Sperm Whale Myoglobin with Hydrogen Peroxide

Alayash, Abdu I.; Ryan, B. A. Brockner; Eich, Raymond F.; Olson, John S.; Cashon, Robert E.

doi:10.1074/jbc.274.4.2029

Cited by 80 publications

(44 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…18,19 However, peroxidase enzymes are prone to inactivation from slow attack of hydrogen peroxide in the absence of other reductant substrates or when the ratio of H 2 O 2 /enzyme is large. 20,21 There are several irreversible damage pathways for heme proteins, including the oxidation of the heme ring and release of free iron, 22-26 the intramolecular cross-linking of amino acid residues, and dimerization or oligomerization of proteins resulting from intra-and inter-molecular radical reactions, 27-32 formation of amino acid peroxyl radicals, 29 Two strategies have been used to protect enzymes from damage by peroxide: (1) an impermeable barrier on the biosensor surface to prevent H 2 O 2 from diffusing into the films; 33 (2) a functional protection layer on the biosensor surface to react with H 2 O 2 to protect enzymes from damage. 34-36 The latter approach shows obvious advantages in selectivity and efficiency, since with the former method the barrier may also completely isolate the device from substrates.…”

Section: Introductionmentioning

confidence: 99%

Protecting Peroxidase Activity of Multilayer Enzyme-Polyion Films Using Outer Catalase Layers

Rusling

2007

J. Phys. Chem. B

View full text Add to dashboard Cite

Films constructed layer-by-layer on electrodes with architecture {protein/hyaluronic acid (HA)} n containing myoglobin (Mb) or horseradish peroxidase (HRP) were protected against protein damage by H 2 O 2 by using outer catalase layers. Peroxidase activity for substrate oxidation requires activation by H 2 O 2 , but {protein/HA} n films without outer catalase layers are damaged slowly and irreversibly by H 2 O 2 . The rate and extent of damage were decreased dramatically by adding outer catalase layers to decompose H 2 O 2 . Comparative studies suggest that protection results from catalase decomposing a fraction of the H 2 O 2 as it enters the film, rather than by an in-film diffusion barrier. The outer catalase layers controlled the rate of H 2 O 2 entry into inner regions of the film, and biased the system to favor electrocatalytic peroxide reduction over enzyme damage. Catalase-protected {protein/ HA} n films had an increased linear concentration range for H 2 O 2 detection. This approach offers an effective way to protect biosensors from damage by H 2 O 2 .

show abstract

Section: Introductionmentioning

confidence: 99%

Protecting Peroxidase Activity of Multilayer Enzyme-Polyion Films Using Outer Catalase Layers

Rusling

2007

J. Phys. Chem. B

View full text Add to dashboard Cite

show abstract

“…Hydrophobic Nature 2 Heme pocket residues are known to affect greatly the heme stability in myoglobin (24,25). We therefore examined the in vivo accumulation of hemecontaining CooA in some CooA variants in order to test whether the introduction of hydrophilic or charged residues at position 113 and/or 116 affected that property.…”

Section: Weakening Thementioning

confidence: 99%

The Role of the Hydrophobic Distal Heme Pocket of CooA in Ligand Sensing and Response

Youn

Kerby

Roberts

2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

CooA from Rhodospirillum rubrum is a heme-containing transcriptional activator that becomes activated only upon binding CO. The basis for this specificity has been probed in a CooA variant, termed ⌬P3R4 CooA, lacking two residues adjacent to the Pro 2 heme ligand, which weakens that ligand. ⌬P3R4 CooA can bind imidazole and CN ؊ , as well as CO, and form a 6-coordinate low spin adduct with each. However, in contrast to the case with CO, imidazole and CN ؊ do not stimulate the DNA binding activity of ⌬P3R4 CooA. This result indicates that the CO-specific activation of CooA is not merely the result of creation of a 6-coordinate CooA adduct but that there must be another element to this response. One feature of CooA activation is modest repositioning of the C-helices upon CO binding, so we altered a portion of the C-helix (residues Ile 113 and Leu 116 ) located near the heme-bound CO in wild type CooA, and we investigated the effect on CO-specific activation. Surprisingly, the sizes of Ile 113 and/or Leu 116 positions are not critical for CooA activation by CO, disproving a precise interaction between these residues and the CO-bound heme as a basis for the CO activation mechanism and CO ligand specificity. In contrast, hydrophobic residues at these positions contribute to the activation. Some CooA variants altered at these positions in the background of ⌬P3R4 were also found to show low but reproducible activation in response to imidazole binding to the heme. A model for the role of hydrophobicity in CooA activation and specificity is suggested.

show abstract

“…It is possible to improve its peroxidase activity by changing the structural orientation in the vicinity of its heme sites. 82 Considering the fact that a noncovalent interaction in a supramolecular assembly system significantly alters the heme orientation, 83 it might be a feasible way to functionally convert Hb to a peroxidase-like enzyme by introducing a membrane environment. SP sephadex is a chromatographic medium for protein purification.…”

Section: ·3 Hemoglobinmentioning

confidence: 99%

Third-Generation Biosensors Based on the Direct Electron Transfer of Proteins

Zhang

2004

ANAL. SCI.

176

View full text Add to dashboard Cite

Recent progress in third-generation electrochemical biosensors based on the direct electron transfer of proteins is reviewed. The development of three generations of electrochemical biosensors is also simply addressed. Special attention is paid to protein-film voltammetry, which is a powerful way to obtain the direct electron transfer of proteins. Research activities on various kinds of biosensors are discussed according to the proteins (enzymes) used in the specific work.

show abstract

Reactions of Sperm Whale Myoglobin with Hydrogen Peroxide

Cited by 80 publications

References 51 publications

Protecting Peroxidase Activity of Multilayer Enzyme-Polyion Films Using Outer Catalase Layers

Protecting Peroxidase Activity of Multilayer Enzyme-Polyion Films Using Outer Catalase Layers

The Role of the Hydrophobic Distal Heme Pocket of CooA in Ligand Sensing and Response

Third-Generation Biosensors Based on the Direct Electron Transfer of Proteins

Contact Info

Product

Resources

About