Microbial resistance to metals in the environment.
TL;DR: Six metal resistance mechanisms exist: exclusion by permeability barrier, intra- and extra-cellular sequestration, active transport efflux pumps, enzymatic detoxification, and reduction in the sensitivity of cellular targets to metal ions.
About: This article is published in Ecotoxicology and Environmental Safety.The article was published on 2000-03-01. It has received 1247 citations till now.
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TL;DR: The current status of microbial synthesis and applications of metal nanoparticles is presented and several factors such as microbial cultivation methods and the extraction techniques have to be optimized and the combinatorial approach such as photobiological methods may be used.
1,472 citations
TL;DR: Biosurfactants are surfactants that are produced extracellularly or as part of the cell membrane by bacteria, yeast and fungi as mentioned in this paper, which are used for soil and water treatment.
1,406 citations
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TL;DR: The synthesis process was quite fast and silver nanoparticles were formed within minutes of silver ion coming in contact with the cell filtrate, and the process of reduction being extracellular and fast may lead to the development of an easy bioprocess for synthesis ofsilver nanoparticles.
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TL;DR: The first bacterial metallothionein cation-binding proteins, which by definition is a small protein that binds metal cations by means of numerous cysteine thiolates, has been characterized in cyanobacteria.
Abstract: Bacterial plasmids encode resistance systems for toxic metal ions including Ag+, AsO2-, AsO4(3-), Cd2+, CO2+, CrO4(2-), Cu2+, Hg2+, Ni2+, Pb2+, Sb3+, TeO3(2-), Tl+, and Zn2+. In addition to understanding of the molecular genetics and environmental roles of these resistances, studies during the last few years have provided surprises and new biochemical mechanisms. Chromosomal determinants of toxic metal resistances are known, and the distinction between plasmid resistances and those from chromosomal genes has blurred, because for some metals (notably mercury and arsenic), the plasmid and chromosomal determinants are basically the same. Other systems, such as copper transport ATPases and metallothionein cation-binding proteins, are only known from chromosomal genes. The largest group of metal resistance systems function by energy-dependent efflux of toxic ions. Some of the efflux systems are ATPases and others are chemiosmotic cation/proton antiporters. The CadA cadmium resistance ATPase of gram-positive bacteria and the CopB copper efflux system of Enterococcus hirae are homologous to P-type ATPases of animals and plants. The CadA ATPase protein has been labeled with 32P from gamma-32P-ATP and drives ATP-dependent Cd2+ uptake by inside-out membrane vesicles. Recently isolated genes defective in the human hereditary diseases of copper metabolism, Menkes syndrome and Wilson's disease, encode P-type ATPases that are more similar to the bacterial CadA and CopB ATPases than to eukaryote ATPases that pump different cations. The arsenic resistance efflux system transports arsenite, using alternatively either a two-component (ArsA and ArsB) ATPase or a single polypeptide (ArsB) functioning as a chemiosmotic transporter. The third gene in the arsenic resistance system, arsC, encodes an enzyme that converts intracellular arsenate [As (V)] to arsenite [As (III)], the substrate of the efflux system. The three-component Czc (Cd2+, Zn2+, and CO2+) chemiosmotic efflux pump of soil microbes consists of inner membrane (CzcA), outer membrane (CzcC), and membrane-spanning (CzcB) proteins that together transport cations from the cytoplasm across the periplasmic space to the outside of the cell. Finally, the first bacterial metallothionein (which by definition is a small protein that binds metal cations by means of numerous cysteine thiolates) has been characterized in cyanobacteria.
1,222 citations
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TL;DR: In addition to the bacteria in the rumen there are many larger organisms which at various times have been designated protozoa, of which there are two groups both in the subclass Trichostomatia and the entodiniomorphs.
Abstract: In addition to the bacteria in the rumen there are many larger (5–250/mm long) organisms which at various times have been designated protozoa Of these the ‘ovals’ (Quin’s and Eadie’s) are now known to be large bacteria (Orpin, 1976) and the ‘flagellates’ Neocallimastix frontalis, Piromonas communis and Sphaeromonas communis are the zoospores of phycomycete fungi (Orpin, 1977a, b) There are genuine flagellates in the rumen, eg Trichomonas spp, Monoceromonas sp and Chilomastix sp, but almost nothing is known about their metabolism (Jensen and Hammon, 1964) The largest, most obvious and most important protozoa are the ciliates, of which there are two groups both in the subclass Trichostomatia The so called ‘holotrich’ protozoa belong to the order Vestibuliferida and the entodiniomorphs to the order Entodiniomorphida, suborder Entodiniomorphina and family Ophryoscolecidae As the properties and metabolism of these two protozoal groups are different, they will be considered separately below
903 citations
TL;DR: Many of the inorganic assemblies that otherwise buttress the structure of biopolymers or catalyze substrate transformation in active sites of enzymes have also been adapted to serve sensor functions in the metalloregulatory proteins.
Abstract: Metalloproteins play structural and catalytic roles in gene expression. The metalloregulatory proteins are a subclass that exerts metal-responsive control of genes involved in respiration, metabolism, and metal-specific homeostasis or stress-response systems, such as iron uptake and storage, copper efflux, and mercury detoxification. Two allosteric mechanisms for control of gene expression were first discovered in metalloregulatory systems: an iron-responsive translational control mechanism for ferritin production and a mercury-responsive DNA-distortion mechanism for transcriptional control of detoxification genes. These otherwise unrelated mechanisms give rise to a rapid physiological response when metal ion concentrations exceed a dangerous threshold. Molecular recognition in these allosteric metal ion receptors is achieved through atypical coordination geometries, cluster formation, or complexes with prosthetic groups, such as sulfide and heme. Thus, many of the inorganic assemblies that otherwise buttress the structure of biopolymers or catalyze substrate transformation in active sites of enzymes have also been adapted to serve sensor functions in the metalloregulatory proteins. Mechanistic studies of these metal-sensor protein interactions are providing new insights into fundamental aspects of inorganic chemistry, molecular biology, and cellular physiology.
602 citations
TL;DR: This review concentrates on bacterial efflux systems for inorganic metal cations and anions, which have generally been found as resistance systems from bacteria isolated from metal-polluted environments.
Abstract: Studying metal ion resistance gives us important insights into environmental processes and provides an understanding of basic living processes. This review concentrates on bacterial efflux systems for inorganic metal cations and anions, which have generally been found as resistance systems from bacteria isolated from metal-polluted environments. The protein products of the genes involved are sometimes prototypes of new families of proteins or of important new branches of known families. Sometimes, a group of related proteins (and presumedly the underlying physiological function) has still to be defined. For example, the efflux of the inorganic metal anion arsenite is mediated by a membrane protein which functions alone in Gram-positive bacteria, but which requires an additional ATPase subunit in some Gram-negative bacteria. Resistance to Cd2+ and Zn2+ in Gram-positive bacteria is the result of a P-type efflux ATPase which is related to the copper transport P-type ATPases of bacteria and humans (defective in the human hereditary diseases Menkes' syndrome and Wilson's disease). In contrast, resistance to Zn2+, Ni2+, Co2+ and Cd2+ in Gram-negative bacteria is based on the action of proton-cation antiporters, members of a newly-recognized protein family that has been implicated in diverse functions such as metal resistance/nodulation of legumes/cell division (therefore, the family is called RND). Another new protein family, named CDF for 'cation diffusion facilitator' has as prototype the protein CzcD, which is a regulatory component of a cobalt-zinc-cadmium resistance determinant in the Gram-negative bacterium Alcaligenes eutrophus. A family for the ChrA chromate resistance system in Gram-negative bacteria has still to be defined.
531 citations
TL;DR: Isolated walls of Bacillus subtilis Marburg, prepared in a manner which avoided metal contamination other than by the growth medium, were incubated in dilute metal solutions, separated by membrane filtration, and monitored by atomic absorption to give uptake data for 18 metals.
Abstract: Isolated walls of Bacillus subtilis Marburg, prepared in a manner which avoided metal contamination other than by the growth medium, were incubated in dilute metal solutions, separated by membrane filtration (0.22 mum), and monitored by atomic absorption to give uptake data for 18 metals. Substantial amounts of Mg2+, Fe3+, Cu2+, Na+, and K+ (amounts which were often visible as Au3+, and Ni2+ (the higher atomic-numbered elements also visible as electron scattering), and small amounts of Hg2+, Sr2+, Pb2+, and Ag+ were taken into the wall. Some (Li+, Ba2+, Co2+, and Al3+) were not absorbed. Most metals which had atomic numbers greater than 11 and which could be detected by electron microscopy appeared to diffusely stain thin sections of the wall. Magnesium, on the other hand, partitioned into the central region, and these sections of walls resisted ruthenium red staining, which was not true for the other metals. Areas of the walls also acted as nucleation sites for the growth of microscopic elemental gold crystals when incubated in solutions of auric chloride. Retention or displacement of the metals was estimated by a "chromatographic" method using the walls cross-linked by the carbodiimide reaction to adipic hydrazide agarose beads (which did not take up metal but reduced the metal binding capacity of the walls by ca. 1%) packed in a column. When a series of 12 metal solutions was passed through the column, it became evident that Mg2+, Ca2+, Fe3+, and Ni2+ were strongly bound to the walls and could be detected by both atomic absorption and by their electron-scattering power in thin sections, qhereas the other metals were fisplaced or replaced. Partial lysozyme digestion of the walls (causing a 28% loss of a [3H]diaminopimelic acid label) greatly diminished the Mg2+ retention but not that of Ca2+, Fe3+, or Ni2+, indicating that there are select sites for various cations.
522 citations