Mössbauer and EPR study of a cytochrome b modelDedicated to Professor F. Dörr on the occasion of his 80th birthday.

Яковлева, О. А.; Reiner, Michael; Rau, Harald K.; Haehnel, Wolfgang; Parak, F.

doi:10.1039/b109570f

Cited by 12 publications

(8 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2A) and EPR spectra (ESI, Fig. S5†) of 2 are indicative of 6-coordinate bis-histidine ligated heme C. 20,21 …”

Section: Resultsmentioning

confidence: 99%

“…Ferric and ferrous UV/visible (Fig.2A) and EPR spectra (ESI, Fig.S5 †) of 2 are indicative of 6-coordinate bis-histidine ligated heme C 20,21. Heme C containing maquette binds O 2 Despite the modications to the original design (1), 2 retains the ability to undergo ligand exchange between the histidine sidechain occupying the 6 th coordination site on heme C and…”

mentioning

confidence: 99%

See 1 more Smart Citation

Constructing a man-made c-type cytochrome maquette in vivo: electron transfer, oxygen transport and conversion to a photoactive light harvesting maquette.

et al. 2014

View full text Add to dashboard Cite

The successful use of man-made proteins to advance synthetic biology requires both the fabrication of functional artificial proteins in a living environment, and the ability of these proteins to interact productively with other proteins and substrates in that environment. Proteins made by the maquette method integrate sophisticated oxidoreductase function into evolutionarily naive, non-computationally designed protein constructs with sequences that are entirely unrelated to any natural protein. Nevertheless, we show here that we can efficiently interface with the natural cellular machinery that covalently incorporates heme into natural cytochromes c to produce in vivo an artificial c-type cytochrome maquette. Furthermore, this c-type cytochrome maquette is designed with a displaceable histidine heme ligand that opens to allow functional oxygen binding, the primary event in more sophisticated functions ranging from oxygen storage and transport to catalytic hydroxylation. To exploit the range of functions that comes from the freedom to bind a variety of redox cofactors within a single maquette framework, this c-type cytochrome maquette is designed with a second, non-heme C, tetrapyrrole binding site, enabling the construction of an elementary electron transport chain, and when the heme C iron is replaced with zinc to create a Zn porphyrin, a light-activatable artificial redox protein. The work we describe here represents a major advance in de novo protein design, offering a robust platform for new c-type heme based oxidoreductase designs and an equally important proof-of-principle that cofactor-equipped man-made proteins can be expressed in living cells, paving the way for constructing functionally useful man-made proteins in vivo.

show abstract

“…2A) and EPR spectra (ESI, Fig. S5†) of 2 are indicative of 6-coordinate bis-histidine ligated heme C. 20,21 …”

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Constructing a man-made c-type cytochrome maquette in vivo: electron transfer, oxygen transport and conversion to a photoactive light harvesting maquette.

et al. 2014

View full text Add to dashboard Cite

show abstract

“…The g zz and A zz are the dominating fine and hyperfine tensor quantities, and this causes the magnetic hyperfine splitting to be determined essentially by the product g zz A zz . It should be noted that Iakovleva et al [63] have reported a heme site in a bisHis coordinated cytochrome b model protein (MOP1), which exhibits an EPR signal similar to those of Type I species, and which they interpreted as a result of a novel spin admixture between the ferric intermediate (S = 3/2) and the low-spin states. However, their Mçssbauer spectroscopic investigation of MOP1 showed that the broadened EPR pattern was caused by spin-spin-relaxation effects between the two heme sites in the model protein.…”

mentioning

confidence: 93%

Low‐Temperature EPR and Mössbauer Spectroscopy of Two Cytochromes with His–Met Axial Coordination Exhibiting HALS Signals

et al. 2006

View full text Add to dashboard Cite

C-type cytochromes with histidine-methionine (His-Met) iron coordination play important roles in electron-transfer reactions and in enzymes. Low-temperature electron paramagnetic resonance (EPR) spectra of low-spin ferric cytochromes c can be divided into two groups, depending on the spread of g values: the normal rhombic ones with small g anisotropy and g(max) below 3.2, and those featuring large g anisotropy with g(max) between 3.3 and 3.8, also denoted as highly axial low spin (HALS) species. Herein we present the detailed magnetic properties of cytochrome c(553) from Bacillus pasteurii (g(max) 3.36) and cytochrome c(552) from Nitrosomonas europaea (g(max) 3.34) over the pH range 6.2 to 8.2. Besides being structurally very similar, cytochrome c(553) shows the presence of a minor rhombic species at pH 6.2 (6 %), whereas cytochrome c(552) has about 25 % rhombic species over pH 7.5. The detailed Mössbauer analysis of cytochrome c(552) confirms the presence of these two low-spin ferric species (HALS and rhombic) together with an 8 % ferrous form with parameters comparable to the horse cytochrome c. Both EPR and Mössbauer data of axial cytochromes c with His-Met iron coordination are consistent with an electronic (d(xy))(2) (d(xz))(2) (d(yz))(1) ground state, which is typical for Type I model hemes.

show abstract

“…27,28 Studies of the metal center in heme proteins and model systems have shown that many factors, including noncovalent interactions, may play important roles in the properties of these metalloproteins. [29][30][31][32] The importance of CH/p interactions of aromatic residues with porphyrin in hemoproteins was shown. 33 It was demonstrated that the noncovalent interactions with the propionic groups of porphyrins are very important for the orientations of the imidazoles and that the conformations of the propionic groups have a strong influence on these interactions.…”

Section: Introductionmentioning

confidence: 99%

π–π and cation–π interactions in protein–porphyrin complex crystal structures

2012

View full text Add to dashboard Cite

In this study we have described the p-p and cation-p interactions between the porphyrin ring and the protein part of porphyrin-containing proteins to better understand their stabilizing role. The number of pp interactions was higher than that of cation-p interactions in the same set of proteins studied. The pyrrole groups of one porphyrin can be involved in p-p interactions with p systems of another porphyrin in the protein. We have found 5.1% cation-p interactions between porphyrin Fe 2+ metal cations and p systems of surrounding amino acids as well as the pyrrole rings of other porphyrins. We observed that most of the p-p interactions have an energy in the range 20.5 to 22.0 kcal mol 21 , while the cation-p interactions showed an energy in the range 22 to 24 kcal mol 21. Further, an appreciable number of metal/cation-p interaction pairs have an energy in the range 26 to 213 kcal mol 21. The preferred parallel-stacked orientation is found to be more stable than a T-shaped structure for the full set of p-p interaction pairs. In the case of cation-p interactions, it was found that 44% of the cation-p interactions involved planar stacking, 37% of the interactions belonged to the oblique category, and the remaining 19% of the interactions were of the orthogonal type. The separation distance between the cation group and the aromatic ring decreases as the interplanar angle decreases. Furthermore, in the present study we have found that 10.4% of p residues and 3.9% of cationic residues were found to have one or more stabilization centers. Amino acids deployed in the environment of porphyrin rings are deposited in helices and coils. The results from this study might be used for structure-based porphyrin protein prediction and as scaffolds for future porphyrin-containing protein design.

show abstract

Mössbauer and EPR study of a cytochrome b modelDedicated to Professor F. Dörr on the occasion of his 80th birthday.

Cited by 12 publications

References 21 publications

Constructing a man-made c-type cytochrome maquette in vivo: electron transfer, oxygen transport and conversion to a photoactive light harvesting maquette.

Constructing a man-made c-type cytochrome maquette in vivo: electron transfer, oxygen transport and conversion to a photoactive light harvesting maquette.

Low‐Temperature EPR and Mössbauer Spectroscopy of Two Cytochromes with His–Met Axial Coordination Exhibiting HALS Signals

π–π and cation–π interactions in protein–porphyrin complex crystal structures

Contact Info

Product

Resources

About