The c-type cytochromes of the gram-positive bacterium Bacillus licheniformis

Woolley, Kevin J.

doi:10.1016/0003-9861(87)90114-7

Cited by 17 publications

(3 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Three types of class I c-type cytochromes have been identified in Gram-positive bacteria: (i) cytochromes fused as integral domains of subunit II in membrane-bound aa 3 -type terminal oxidases, (ii) cytochromes bound to the membrane through an Nterminal hydrophobic polypeptide, and (iii) cytochromes bound to the membrane via a diacyl-glyceryl-cysteine moiety (1). The difficulties associated with the study of such water-insoluble proteins may explain why only a few c-type cytochromes have been isolated from Gram-positive bacteria (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13). As a consequence, their properties and functional roles are scarcely known, and no structural information is available, in contrast with cytochromes from Gram-negative bacteria and eukaryotes (14,15).…”

mentioning

confidence: 99%

Crystal Structure of Oxidized Bacillus pasteurii Cytochrome c₅₅₃ at 0.97-Å Resolution

et al. 2000

View full text Add to dashboard Cite

This article reports the first X-ray structure of the soluble form of a c-type cytochrome isolated from a Gram-positive bacterium. Bacillus pasteurii cytochrome c(553), characterized by a low reduction potential and by a low sequence homology with cytochromes from Gram-negative bacteria or eukaryotes, is a useful case study for understanding the structure-function relationships for this class of electron-transfer proteins. Diffraction data on a single crystal of cytochrome c(553) were obtained using synchrotron radiation at 100 K. The structure was determined at 0.97-A resolution using ab initio phasing and independently at 1.70 A in an MAD experiment. In both experiments, the structure solution exploited the presence of a single Fe atom as anomalous scatterer in the protein. For the 0.97-A data, the phasing was based on a single data set. This is the most precise structure of a heme protein to date. The crystallized cytochrome c(553) contains only 71 of the 92 residues expected from the intact protein sequence, lacking the first 21 amino acids at the N-terminus. This feature is consistent with previous evidence that this tail, responsible for anchoring the protein to the cytoplasm membrane, is easily cleaved off during the purification procedure. The heme prosthetic group in B. pasteurii cytochrome c(553) is surrounded by three alpha-helices in a compact arrangement. The largely exposed c-type heme group features a His-Met axial coordination of the Fe(III) ion. The protein is characterized by a very asymmetric charge distribution, with the exposed heme edge located on a surface patch devoid of net charges. A structural search of a representative set of protein structures reveals that B. pasteurii cytochrome c(553) is most similar to Pseudomonas cytochromes c(551), followed by cytochromes c(6), Desulfovibrio cytochrome c(553), cytochromes c(552) from thermophiles, and cytochromes c from eukaryotes. Notwithstanding a low sequence homology, a structure-based alignment of these cytochromes shows conservation of three helical regions, with different additional secondary structure motifs characterizing each protein. In B. pasteurii cytochrome c(553), these motifs are represented by the shortest interhelix connecting fragments observed for this group of proteins. The possible relationships between heme solvent accessibility and the electrochemical reduction potential are discussed.

show abstract

mentioning

confidence: 99%

Crystal Structure of Oxidized Bacillus pasteurii Cytochrome c₅₅₃ at 0.97-Å Resolution

et al. 2000

View full text Add to dashboard Cite

show abstract

“…However, the specific functions related to the alkaline adaptation have not yet been clarified. To understand the molecular features of the intact protein, it is indispensable to consider the function of cytochrome c. Some of the cytochromes c from Bacillaceae strains have been reported to be in soluble forms due to the lacking of an N-terminal sequence associated with intrinsic protease activity (Yamaguchi et al, 1966;Miki and Okunuki, 1969a,b;Woolley, 1987;Davidson et al, 1988;Benini et al, 1998Benini et al, , 2000. Although the purification of a protein using a cocktail of protease inhibitors is promising, the inhibitors do not always inhibit protease activity adequately.…”

Section: Characteristics Of Cytochrome C Expression Following Bacteri...mentioning

confidence: 99%

Differences in Bioenergetic Metabolism of Obligately Alkaliphilic Bacillaceae Under High pH Depend on the Aeration Conditions

et al. 2022

View full text Add to dashboard Cite

Alkaliphilic Bacillaceae appear to produce ATP based on the H+-based chemiosmotic theory. However, the bulk-based chemiosmotic theory cannot explain the ATP production in alkaliphilic bacteria because the H+ concentration required for driving ATP synthesis through the ATPase does not occur under the alkaline conditions. Alkaliphilic bacteria produce ATP in an H+-diluted environment by retaining scarce H+ extruded by the respiratory chain on the outer surface of the membrane and increasing the potential of the H+ for ATP production on the outer surface of the membrane using specific mechanisms of ATP production. Under high-aeration conditions, the high ΔΨ (ca. -170 mV) of the obligate alkaliphilic Evansella clarkii retains H+ at the outer surface of the membrane and increases the intensity of the protonmotive force (Δp) per H+ across the membrane. One of the reasons for the production of high ΔΨ is the Donnan potential, which arises owing to the induction of impermeable negative charges in the cytoplasm. The intensity of the potential is further enhanced in the alkaliphiles compared with neutralophiles because of the higher intracellular pH (ca. pH 8.1). However, the high ΔΨ observed under high-aeration conditions decreased (∼ -140 mV) under low-aeration conditions. E. clarkii produced 2.5–6.3-fold higher membrane bound cytochrome c in the content of the cell extract under low-aeration conditions than under high-aeration conditions. The predominant membrane-bound cytochrome c in the outer surface of the membrane possesses an extra Asn-rich segment between the membrane anchor and the main body of protein. This structure may influence the formation of an H+-bond network that accumulates H+ on the outer surface of the membrane. Following accumulation of the H+-bond network producing cytochrome c, E. clarkii constructs an H+ capacitor to overcome the energy limitation of low aeration at high pH conditions. E. clarkii produces more ATP than other neutralophilic bacteria by enhancing the efficacy per H+ in ATP synthesis. In low H+ environments, E. clarkii utilizes H+ efficiently by taking advantage of its high ΔΨ under high-aeration conditions, whereas under low-aeration conditions E. clarkii uses cytochrome c bound on its outer surface of the membrane as an H+ capacitor.

show abstract

“…Several small 'soluble' Bacillus cytochromes c have been purified; c-551 and c-554 from B. subtilis [21], c-550 from thermophilic Bacillus PS3 [22], c-552 from alkaliphilic B. firmus RAB [23], and c-551, c-552 and c-554 from B. licheniformis [24]. These cytochromes are probably derived from membrane-bound forms by proteolysis.…”

Section: Small Cytochrome C In Bacillusmentioning

confidence: 99%

Membrane-boundBacilluscytochromescand their phylogenetic position among bacterial class I cytochromesc

Sone

Toh

1994

FEMS Microbiology Letters

View full text Add to dashboard Cite

Gram-positive bacteria lack a periplasmic compartment and contain only membrane-bound cytochromes c. There are at least two types. One is found in subunit II of cytochrome oxidase, and the other is small cytochrome c which is also membrane-bound because of an unprocessed signal sequence or post-translational acylation at the N-terminal end of the protein. These Bacillus cytochromes c are compared with known class I cytochromes c, and a phylogenetic tree has been constructed by the neighbour-joining method.

show abstract

The c-type cytochromes of the gram-positive bacterium Bacillus licheniformis

Cited by 17 publications

References 18 publications

Crystal Structure of Oxidized Bacillus pasteurii Cytochrome c₅₅₃ at 0.97-Å Resolution

Crystal Structure of Oxidized Bacillus pasteurii Cytochrome c₅₅₃ at 0.97-Å Resolution

Differences in Bioenergetic Metabolism of Obligately Alkaliphilic Bacillaceae Under High pH Depend on the Aeration Conditions

Membrane-boundBacilluscytochromescand their phylogenetic position among bacterial class I cytochromesc

Contact Info

Product

Resources

About

The c-type cytochromes of the gram-positive bacterium Bacillus licheniformis

Cited by 17 publications

References 18 publications

Crystal Structure of Oxidized Bacillus pasteurii Cytochrome c553 at 0.97-Å Resolution

Crystal Structure of Oxidized Bacillus pasteurii Cytochrome c553 at 0.97-Å Resolution

Differences in Bioenergetic Metabolism of Obligately Alkaliphilic Bacillaceae Under High pH Depend on the Aeration Conditions

Membrane-boundBacilluscytochromescand their phylogenetic position among bacterial class I cytochromesc

Contact Info

Product

Resources

About

Crystal Structure of Oxidized Bacillus pasteurii Cytochrome c₅₅₃ at 0.97-Å Resolution

Crystal Structure of Oxidized Bacillus pasteurii Cytochrome c₅₅₃ at 0.97-Å Resolution