Periplasmic space bacteria

Gram-negative organisms produce ced-bound P-lactamases which reside in the periplasmic space. Thus, for gram-negative bacteria, the antibiotic must penetrate the outer ced membrane/wad before coming in contact with a P-lactamase (80,139,140). 

Gram-negative bacteria are surrounded by two membranes, an inner plasma membrane and an outer membrane. These are separated by a periplasmic space. Most plasma membrane proteins contain long, continuous sequences of about 20 hydrophobic residues that are typical of transmembrane a helices such as those found in bacteriorhodopsin. In contrast, most outer membrane proteins do not show such sequence patterns. 

AGAC-modifying enzymes are active outside the cytoplasmic membrane, in the periplasmic space in Gram-negative bacteria and extracellularly in Gram-positives. Table 9.4 summarizes some of the enzymes involved in AGAC resistance and their spectrum of activity. 

In Gram-negative bacteria which are characterised by a rather complex cell envelope, the CM is also referred to as inner membrane to distinguish it from a second lipid bilayer, termed outer membrane (OM). The space between these two layers is called the periplasm (PP). In the periplasmic space, many proteins are found with a variety of functions. Some are involved in biosynthesis and/or export of cell wall components and surface structures (e.g. pili, flagellae,... 

The uptake of siderophore-iron complexes by Gram-negative bacteria is energy dependent and occurs via specific outer membrane proteins. In the periplasmic space, it binds to its cognate periplasmic binding protein and is then actively transported across the cytoplasmic membrane by an ATP-trans-porter protein. Three principal mechanisms for transport through the outer membrane have been described ... 

The disposition of the different metal centres of bovine heart CcOx is represented in Figure 14.9. The dimetallic CuA site receives electrons directly from cytochrome c, and is located in a globular domain of subunit II, which protrudes into the intermembrane space (the periplasmic space in bacteria). This centre, which was widely believed to be mononuclear is a dicopper site (Figure 14.10) in which the coppers are bridged by two cysteine sul-furs each copper in addition has two other protein ligands. In the one electron-reduced form,... 

Denitrifying bacteria produce one or the other of two usually soluble but very dissimilar nitrite reductases, heme- and Cu-containing types (Brittain et al., 1992 Coyne et al., 1989), both of which are found in the periplasmic space of gram-negative bacteria (Coyne et al., 1990). 

Although the Cu-type family of nitrite reductase is comprised of soluble enzyme and localized in the periplasmic space in gram-negative bacteria, it has proved to be a membrane-bound enzyme in denitrifying Bacillus, which is gram positive and lacks an outer membrane and periplasmic space (Denariaz et ai, 1991 Urata and Satoh, 1991 Ho etal., 1993). 

Bacteria can target proteins to their inner or outer membranes, to the periplasmic space between these membranes, or to the extracellular medium. They use signal sequences at the amino terminus of the proteins (Fig. 

The plasma membrane of bacterial cells, other than the wall-less mycoplasmas and some archaebacteria, is surrounded by a multilayered wall which may be separated from the membrane by a thin periplasm (or periplasmic space). This can be seen most clearly in suitably prepared thin sections of cells of E. coli or other gram-negative bacteria as a relatively empty space of 11- to 25-nm thickness (Fig. 8-28).579 581 The volume of this space (which may be filled with gelled material) depends upon the osmotic pressure of the medium. In E. coli it contains 20-40% of the total... 

Unlike transport across the membranes of the ER, transport across plasma membranes of bacteria often requires both hydrolysis of ATP and energy provided by the membrane electrical potential.33 38 44-48 Secretion into the periplasmic space has been well characterized but less is known about transport of proteins into the external membranes of E. coli48 A16 kDa periplasmic chaperone may be required.483... 

Cyclic photophosphorylation in purple bacteria. QH2 is eventually dehydrogenated in the cytochrome bc1 complex, and the electrons can be returned to the reaction center by the small soluble cytochrome c2, where it reduces the bound tetraheme cytochrome or reacts directly with the special pair in Rhodobacter spheroides. The overall reaction provides for a cyclic photophosphorylation (Fig. 23-32) that pumps 3-4 H+ across the membrane into the periplasmic space utilizing the energy of the two photoexcited electrons. 

How are the possible choices for newly formed proteins made Much seems to depend upon the amino acid sequences at the ends of the polypeptide chains. As they emerge from a ribosome, some N-terminal signal sequences bind to recognition proteins. One such protein labels the ends of proteins destined for secretion into the vesicles of the ER. This protein ensures that the protein end binds to the signal recognition particle (SRP), enters a translocon pore, and undergoes cotranslational passage into the periplasmic space in bacteria or the ER in eukaryotes. Cotranslational modification reactions also occur both in the... 

The processes by which proteins are selected for secretion into the periplasmic space of bacteria or into the vesicles of the endoplasmic reticulum of eukaryotic cells are similar and have been discussed in Chapter 10 (pp. 519-521). However, some details are still being worked out. The first step in translocation is binding of the N terminus of a protein that is emerging from a ribosome to the signal recognition parti-cje 563,564 j le core 0f this particle has a universally conserved structure consisting of two proteins and an RNA molecule.565 571 b... 

The host bacteria used for production of recombinant proteins are usually E. coli, or Bacillus subtilis they may express proteins at 1 % to over 50% of the cellular protein, depending on such variables as the source, promoter structure, and vector type. Generally the proteins are expressed intracellularly, but leader sequences for excretion may be included. In the latter case, the protein is generally excreted into the periplasmic space, which limits the amount that can be produced. Excretion from grampositive species such as B. subtilis sends the product into the culture medium, with little feedback limitation on total expression level. 

The outer membrane of Gram-negative bacteria is spanned by porins, trimeric proteins that form inlet channels between the outer membrane and the periplasmic space. The geometry of the porins defines the substrate uptake limit, which is on the order of 600 daltons (Weiss et al., 1991), approximately equivalent to a trisaccharide. Substrates larger than this limit (with few exceptions) must be hydrolyzed outside the outer membrane prior to uptake. Extracellular hydrolysis is carried out by means of extracellular en-... 

The role of PQQ as cofactor has been established unequivocally only for a number of dehydrogenases that are located in the periplasmic space of gram-negative bacteria [3] (Table 1). These enzymes are involved in the oxidation of alcohols and sugars (to aldehydes and sugar lactones or ketosugars, respectively), especially in processes known as incomplete microbial oxidations [47] (production... 

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