Crystallographic and Spectroscopic Studies of Peroxide-derived Myoglobin Compound II and Occurrence of Protonated FeIV–O

Hersleth, H.-P.; Uchida, Takeshi; Røhr, Åsmund K.; Teschner, Thomas; Schünemann, Volker; Kitagawa, Teizo; Trautwein, Alfred X.; Görbitz, Carl Henrik; Andersson, Karin

doi:10.1074/jbc.m701948200

Cited by 56 publications

(72 citation statements)

References 130 publications

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“…For horse (Equus caballus) deoxy-Mb structure, we used PDB code 2V1K and due to the non-availability of horse oxy-Mb, we transferred the oxygen molecule coordinates from sperm whale oxy-Mb (PDB ID 1MBO) to the deoxy-Mb of horse (46,47). To attain equilibrium and stability, we performed MD simulations on the generated oxy-Mb complex for a period of 10 ns before using the model for docking studies.…”

Section: Methodsmentioning

confidence: 99%

Novel Molecular Interactions of Acylcarnitines and Fatty Acids with Myoglobin

Chintapalli

Jayanthi

Mallipeddi

et al. 2016

Journal of Biological Chemistry

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Edited by George CarmanPrevious research has indicated that long-chain fatty acids can bind myoglobin (Mb) in an oxygen-dependent manner. This suggests that oxy-Mb may play an important role in fuel delivery in Mb-rich muscle fibers (e.g. type I fibers and cardiomyocytes), and raises the possibility that Mb also serves as an acylcarnitinebinding protein. We report for the first time the putative interaction and affinity characteristics for different chain lengths of both fatty acids and acylcarnitines with oxy-Mb using molecular dynamic simulations and isothermal titration calorimetry experiments. We found that short-to medium-chain fatty acids or acylcarnitines (ranging from C2:0 to C10:0) fail to achieve a stable conformation with oxy-Mb. Furthermore, our results indicate that C12:0 is the minimum chain length essential for stable binding of either fatty acids or acylcarnitines with oxyMb. Importantly, the empirical lipid binding studies were consistent with structural modeling. These results reveal that: (i) the lipid binding affinity for oxy-Mb increases as the chain length increases (i.e. C12:0 to C18:1), (ii) the binding affinities of acylcarnitines are higher when compared with their respective fatty acid counterparts, and (iii) both fatty acids and acylcarnitines bind to oxy-Mb in 1:1 stoichiometry. Taken together, our results support a model in which oxy-Mb is a novel regulator of longchain acylcarnitine and fatty acid pools in Mb-rich tissues. This has important implications for physiological fuel management during exercise, and relevance to pathophysiological conditions (e.g. fatty acid oxidation disorders and cardiac ischemia) where long-chain acylcarnitine accumulation is evident.

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Section: Methodsmentioning

confidence: 99%

Novel Molecular Interactions of Acylcarnitines and Fatty Acids with Myoglobin

Chintapalli

Jayanthi

Mallipeddi

et al. 2016

Journal of Biological Chemistry

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“…3, a, with a FeÀO bond of 2.1 , which is ca. 0.1 shorter than in the high-spin ferric metMb state [12] [62]. The cryoradiolytic-induced conversion from ferric metMb to aqua/hydroxy-ferrous Mb can, in crystals, be followed with singlecrystal microspectrophotometry as seen in Fig.…”

mentioning

confidence: 98%

The Influence of X‐Rays on the Structural Studies of Peroxide‐Derived Myoglobin Intermediates

Hersleth

Hsiao

Ryde

et al. 2008

Chemistry & Biodiversity

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In recent years, the awareness of potential radiation damage of metal centers in protein crystals during crystallographic data collection has received increasing attention. The radiation damage can lead to radiation-induced changes and reduction of the metal sites. One of the research fields where these concerns have been comprehensively addressed is the study of the reaction intermediates of the heme peroxidase and oxygenase reaction cycles. For both the resting states and the high-valent intermediates, the X-rays used in the structure determination have given undesired side effects through radiation-induced changes to the trapped intermediates. However, X-rays have been used to generate and trap the peroxy/hydroperoxy state in crystals. In this review, the structural work and the influence of X-rays on these intermediates in myoglobin are summarized and viewed in light of analogous studies on similar intermediates in peroxidases and oxygenases.

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“…The two proteins have similar molecular weights, but quite different content of histidine (His) residues. Myoglobin [Protein Data Bank (PDB) code, 2V1E] contains 11 His residues, 42 whereas there is only one His in lysozyme sequence (PDB code, 2VB1). 43 Therefore, the two proteins are good representatives of His-rich and His-poor proteins for investigating the metal-chelate affinity for His, because the transition metal ions coordinate favorably with aromatic nitrogen atoms with the imidazole group of histidine.…”

Section: Protein Extraction and Back Extractionmentioning

confidence: 99%

A metal‐chelate affinity reverse micellar system for protein extraction

Dong¹,

Meng²,

Feng³

et al. 2009

Biotechnology Progress

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A new nonionic reverse micellar system is developed by blending two nonionic surfactants, Triton X-45 and Span 80. At total surfactant concentrations lower than 60 mmol/L and molar fractions of Triton X-45 less than 0.6, thermodynamically stable reverse micelles of water content (W(0)) up to 30 are formed. Di(2-ethylhexyl) phosphoric acid (HDEHP; 1-2 mmol/L) is introduced into the system for chelating transition metal ions that have binding affinity for histidine-rich proteins. HDEHP exists in a dimeric form in organic solvents and a dimer associated with one transition metal ion, including copper, zinc, and nickel. The copper-chelate reverse micelles (Cu-RM) are characterized for their W(0), hydrodynamic radius (R(h)), and aggregation number (N(ag)). Similar with reverse micelles of bis-2-ethylhexyl sodium sulfosuccinate (AOT), R(h) of the Cu-RM is also linearly related to W(0). However, N(ag) is determined to be 30-90 at W(0) of 5-30, only quarter to half of the AOT reverse micelles. Then, selective metal-chelate extraction of histidine-rich protein (myoglobin) by the Cu-RM is successfully performed with pure and mixed protein systems (myoglobin and lysozyme). The solubilized protein can be recovered by stripping with imidazole or ethylinediaminetetraacetic acid (EDTA) solution. Because various transition metal ions can be chelated to the reverse micelles, it is convinced that the system would be useful for application in protein purification as well as simultaneous isolation and refolding of recombinant histidine-tagged proteins expressed as inclusion bodies.

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Crystallographic and Spectroscopic Studies of Peroxide-derived Myoglobin Compound II and Occurrence of Protonated FeIV–O

Cited by 56 publications

References 130 publications

Novel Molecular Interactions of Acylcarnitines and Fatty Acids with Myoglobin

Novel Molecular Interactions of Acylcarnitines and Fatty Acids with Myoglobin

The Influence of X‐Rays on the Structural Studies of Peroxide‐Derived Myoglobin Intermediates

A metal‐chelate affinity reverse micellar system for protein extraction

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