Magnetic-circular-dichroism studies of haem a and its derivatives.
Ontology highlight
ABSTRACT:
SUBMITTER: Brittain T
PROVIDER: S-EPMC1185793 | biostudies-other | 1978 Aug
REPOSITORIES: biostudies-other
Similar Datasets
Project description:myo-Inositol oxygenase (MIOX) catalyzes the 4e(-) oxidation of myo-inositol (MI) to D-glucuronate using a substrate activated Fe(II)Fe(III) site. The biferrous and Fe(II)Fe(III) forms of MIOX were studied with circular dichroism (CD), magnetic circular dichroism (MCD), and variable temperature variable field (VTVH) MCD spectroscopies. The MCD spectrum of biferrous MIOX shows two ligand field (LF) transitions near 10000 cm(-1), split by ~2000 cm(-1), characteristic of six coordinate (6C) Fe(II) sites, indicating that the modest reactivity of the biferrous form toward O2 can be attributed to the saturated coordination of both irons. Upon oxidation to the Fe(II)Fe(III) state, MIOX shows two LF transitions in the ~10000 cm(-1) region, again implying a coordinatively saturated Fe(II) site. Upon MI binding, these split in energy to 5200 and 11200 cm(-1), showing that MI binding causes the Fe(II) to become coordinatively unsaturated. VTVH MCD magnetization curves of unbound and MI-bound Fe(II)Fe(III) forms show that upon substrate binding, the isotherms become more nested, requiring that the exchange coupling and ferrous zero-field splitting (ZFS) both decrease in magnitude. These results imply that MI binds to the ferric site, weakening the Fe(III)-?-OH bond and strengthening the Fe(II)-?-OH bond. This perturbation results in the release of a coordinated water from the Fe(II) that enables its O2 activation.
| S-EPMC3882275 | biostudies-literature
Project description:Calprotectin (CP) is an abundant metal-chelating protein involved in host defense, and the ability of human CP to bind Fe(ii) in a calcium-dependent manner was recently discovered. In the present study, near-infrared magnetic circular dichroism spectroscopy is employed to investigate the nature of Fe(ii) coordination at the two transition-metal-binding sites of CP that are a His3Asp motif (site 1) and a His6 motif (site 2). Upon the addition of sub-stoichiometric Fe(ii), a six-coordinate (6C) Fe(ii) center associated with site 2 is preferentially formed in the presence of excess Ca(ii). This site exhibits an exceptionally large ligand field (10Dq = 11 045 cm-1) for a non-heme Fe(ii) protein. Analysis of CP variants lacking residues of the His6 motif supports that CP coordinates Fe(ii) at site 2 by employing six His ligands. In the presence of greater than one equiv. of Fe(ii) or upon mutation of the His6 motif, the metal ion also binds at site 1 of CP to form a five-coordinate (5C) Fe(ii)-His3Asp motif that was previously unidentified in this system. Notably, the introduction of His-to-Ala mutations at the His6 motif results in a mixture of 6C (site 2) and 5C (site 1) signals in the presence of sub-stoichiometric Fe(ii). These results are consistent with a reduced Fe(ii)-binding affinity of site 2 as more weakly coordinating water-derived ligands complete the 6C site. In the absence of Ca(ii), both sites 1 and 2 are occupied upon addition of sub-stoichiometric Fe(ii), and a stronger ligand field is observed for the 5C site. These spectroscopic studies provide further evaluation of a unique non-heme Fe(ii)-His6 site for metalloproteins and support the notion that Ca(ii) ions influence the Fe(ii)-binding properties of CP.
| S-EPMC5361872 | biostudies-literature
Project description:A detailed study of the effect of temperature on the m.c.d. (magnetic circular dichroism) spectra of cytochrome c oxidase and some of its derivatives was undertaken to characterize the spin states of haem a and a(3). The fully reduced enzyme contains haem a(3) (2+) in its high-spin form and haem a(2+) in the low-spin state. This conclusion is reached by comparing the spectrum with that of the mixed-valence CO derivatives and its photolysis product. The cyanide derivative of the fully reduced enzyme contains both haem a and a(3) in the low-spin ferrous form. The m.c.d. spectra of the fully oxidized derivatives are consistent with the presence of one low-spin ferric haem group, assigned to a, which remains unaltered in the presence of ligands. Haem a(3) is high spin in the resting enzyme and the fluoride derivatives, and low spin in the cyanide form. The partially reduced formate and cyanide derivatives have temperature-dependent m.c.d. spectra due to the presence of high- and low-spin haem a(3) (3+) respectively. Haem a is low-spin ferrous in both. A comparison of the magnitude of the temperature-dependence of haem a(3) (3+) in the fully oxidized and partially reduced forms shows a marked difference which is tentatively ascribed to the presence of anti-ferromagnetic coupling in the fully oxidized form of the enzyme, and to its absence from the partially reduced derivatives, owing to the reduction of both Cu(2+) ions.
| S-EPMC1164905 | biostudies-other
Project description:Native and reconstituted myoglobin were prepared and their c.d. spectra recorded in the Soret region. Time-dependent changes in dichroism following reconstitution were observed and related to haem orientational disorder. Comparative c.d. studies, in agreement with n.m.r. studies, reveal that the degree and nature of this disorder are species-dependent.
| S-EPMC1147030 | biostudies-other
Project description:M.c.d. (magnetic-circular-dichroism) spectroscopy was used to study the magnetization properties of the haem centres in cytochrome c oxidase with magnetic fields of between 0 and 5.3 T over the temperature range 1.5--200 K. The oxidized, oxidized cyanide and partially reduced cyanide forms of the enzyme were studied. In the oxidized state only cytochrome a3+ is detectable by m.c.d. spectroscopy, and its magnetization characteristics show it to be a low-spin ferric haem. In the partially reduced cyanide form of the enzyme cytochrome a is in the diamagnetic low-spin ferrous form, whereas cytochrome a3--CN is e.p.r.-detectable and gives an m.c.d.-magnetization curve typical of a low-spin ferric haem. In the oxidized cyanide form of the enzyme both cytochrome a and cytochrome a3--CN are detectable by m.c.d. spectroscopy, although only cytochrome a gives an e.p.r. signal. The magnetization characteristics of haem a3--CN show clearly that its ground state is an electronic doublet and that another state, probably a spin singlet, lies greater than 10 cm-1 above this. These features are well accounted for by an electronic state of spin S = 1 with a predominantly axial distortion, which leaves the doublet, Ms = +/- 1, as the ground state and the component Ms = 0 as the excited state. This state would not give an e.p.r. signal. Such an electronic state could arise either from a ferromagnetic coupling between haem a3+(3)-CN and the cupric ion, Cua3, or form a haem in the Fe(IV) state.
| S-EPMC1162656 | biostudies-other
Project description:The spin states of the haem components of mixed-valence cytochrome oxidase were studied at room temperature and at temperature down to 20K by using magnetic circular dichroism. The room-temperature studies show the presence of a low-spin ferrous haem together with a low-spin ferric haem, which we attribute to heams a3 and a respectively. At temperatures below 100K it appears that the CO of the mixed-valence CO complex may be irreversibly photolysed, and that in this case haems a and a3 assume their high-spin states. Thus in this enzyme haem-haem interactions appear possible at temperatures below 100K.
| S-EPMC1164187 | biostudies-other
Project description:The reaction product of myoglobin and H2O2 exists in two different forms according to the external pH. Varied-temperature magnetic-circular dichroism (m.c.d.) spectroscopy demonstrates that both contain the oxyferryl ion Fe(IV) = O. Alkaline myoglobin peroxide has often been used as a model for oxidized intermediates in the catalytic cycles of haem-containing peroxidases, but absorption and m.c.d. spectra show that the acid form is much more closely related to species such as horeradish peroxidase Compound II. The differences are tentatively ascribed to ionization of the proximal histidine ligand in alkaline myoglobin peroxide. It is also shown that the m.c.d. method allows an estimate of the zero-field splitting parameter of both forms, values of D = 28.0 +/- 3 cm-1 and 35.0 +/- 5 cm-1 being obtained for the alkaline and acid forms respectively.
| S-EPMC1138856 | biostudies-other
Project description:Circular dichroism (CD) signals revealed in some materials may arise from different origins during measurements. Magnetic field dependent CD (MCD) emanating from the spin-polarized band provides direct insight into the spin-spin interband transitions in magnetic materials. On the contrary, natural CD effects which are artefactual signals resulting from the linear polarization (LP) components during the polarization modulation with a photo-elastic modulator in anisotropic polymer systems were usually observed. There is no simple method to reliably distinguish MCD effect due to spin polarized band structures from natural CD effect, which limits our understanding of the magnetic material/polymer hybrid structures. This paper aims to introduce a general strategy of averaging out the magnetic linear dichroism (MLD) contributions due to the anisotropic structure and disentangling MCD signal(s) from natural MCD signal(s). We demonstrate the effectiveness of separating MCD from natural MCD using rotational MCD measurement and presented the results of a sample with Co thin film on polymer Scotch tape (unplasticized polyvinyl chloride) glued on a quartz substrate. We demonstrate that the proposed method can be used as an effective tool in disentangling MCD and natural MCD effects, and it opens prospects to study the magnetic material /polymer hybrid systems.
| S-EPMC6868135 | biostudies-literature
Project description:Absorption and magnetic circular dichroism (MCD) spectra have been measured and theoretically simulated for a series of palladium octaethylporphyrins substituted at the meso positions with phenyl groups (n = 0-4). Analysis of the spectra included the perimeter model and time-dependent density functional theory (TDDFT) calculations. With the increasing number of phenyl substituents, the molecule is transformed from a positive hard (ΔHOMO > ΔLUMO) to a soft (ΔHOMO ≈ ΔLUMO) chromophore. This is manifested by a drastic decrease of the absorption intensity in the 0-0 region of the Q-band and by the strongly altered ratio of MCD intensities in the Q and Soret regions. Such behavior can be readily predicted using perimeter model, by analyzing frontier orbital shifts caused by various perturbations: alkyl and aryl substitution, insertion of a metal, and deviations from planarity. TDDFT calculations confirm the trends predicted by the perimeter model, but they fail in cases of less symmetrical derivatives to properly reproduce the MCD spectra in the Soret region. Our results confirm the power of the perimeter model in predicting absorption and MCD spectra of large organic molecules, porphyrins in particular. We also postulate, contrary to previous works, that the isolated porphyrin dianion is not a soft chromophore, but rather a strongly positive-hard one.
| S-EPMC7584373 | biostudies-literature
Project description:The efficiency of photosynthetic light energy conversion depends largely on the molecular architecture of the photosynthetic membranes. Linear- and circular-dichroism (LD and CD) studies have contributed significantly to our knowledge of the molecular organization of pigment systems at different levels of complexity, in pigment-protein complexes, supercomplexes, and their macroassemblies, as well as in entire membranes and membrane systems. Many examples show that LD and CD data are in good agreement with structural data; hence, these spectroscopic tools serve as the basis for linking the structure of photosynthetic pigment-protein complexes to steady-state and time-resolved spectroscopy. They are also indispensable for identifying conformations and interactions in native environments, and for monitoring reorganizations during photosynthetic functions, and are important in characterizing reconstituted and artificially constructed systems. This educational review explains, in simple terms, the basic physical principles, and theory and practice of LD and CD spectroscopies and of some related quantities in the areas of differential polarization spectroscopy and microscopy.
| S-EPMC2744782 | biostudies-literature