The decentralized administrations are the third level of administrative divisions in Greece. They were created in January 2011 as part of a far-reaching reform of the country's administrative structure, the Kallikratis reform, they enjoy both administrative and financial autonomy and exercise devolved state powers in urban planning and energy policy, forestry and citizenship. Beyond that, they are tasked with supervising the first and second-level self-governing bodies: the municipalities and regions, they are run by a government-appointed general secretary, assisted by an advisory council drawn from the regional governors and the representatives of the municipalities. Decentralized Administration of Attica, with the capital of Athens Decentralized Administration of Macedonia and Thrace, with the capital of Thessaloniki Decentralized Administration of Epirus and Western Macedonia, with the capital of Ioannina Decentralized Administration of Thessaly and Central Greece, with the capital of Larissa Decentralized Administration of Peloponnese, Western Greece and the Ionian, with the capital of Patras Decentralized Administration of the Aegean, with the capital of Piraeus Decentralized Administration of Crete, with the capital of Heraklion Autonomous Monastic State of Mount Athos, Ministry of Interior.
"Structure and operation of local and regional democracy". Council of Europe
Brendan O. McGonigle was a reader in psychology at the University of Edinburgh in Scotland, he received a PhD from Queen's University Belfast, Northern Ireland. In 1964 he did his postdoc at Durham University, moving in 1965 to lecture in experimental psychology at Oxford University. Following a stint as an assistant professor and NIH Research Associate at the Animal Behaviour Lab, Pennsylvania State University, he moved to the University of Edinburgh in 1969. Brendan died on 29 November 2007.. Brendan's main interest was in characterising the growth and dynamics of intelligent systems. Research on this involved comparative psychology, developmental psychology and cognitive modelling, all integrated within one programme. Research with squirrel monkeys, capuchin monkeys, young children studied pre-linguistic competencies. Monkeys provided inspiration for robotic models of complex primate intelligence. A central focus was the search for cognitive tasks which could be used in humans. Brendan's work was borne from the animal learning culture of the 1960s, but he pioneered the study of more complex relational rule learning in animals by moving away from the simple two-choice discrimination paradigm characteristic of associationistic approaches to animal minds.
A well known study with Margaret Chalmers published in Nature adapted a test of transitive reasoning for monkeys and showed that monkeys were capable of performing on these tasks at comparable levels of success to young children. The authors argued that both species were evincing rational choice based on linear ordering of information and confirmed this using reaction time measures. In his research, Brendan was concerned to allow monkeys long-term learning opportunities comparable to that available for children, so his subsequent work with Cebus apella was a long and staged programme in which the monkeys were trained to seriate by size and classify by shape and colour up to 12 objects on a touch screen – a level of ordering competence that only emerges in human development at around 6/7 years of age and had never before been demonstrated in a non-human species; the sequences achieved by Cebus apella have significance for the evolution of human language. Although the monkeys were trained on a core spine such as square, triangle, they transferred to extended versions such as "touch all the stars all the triangles all the hexagons" with an ease that could not be predicted by simple association learning.
They nested size relations within these classes, choosing for example large star, middle sized star, small star, large hexagon, middle sized hexagon, etc. At the end of their training the monkeys were able to maintain 4 different sequences that randomly alternated on different trials: 9 stars ordered by size, 9 hexagons ordered by size and 9 triangles ordered by size, as well as a 9 item set composed of all three shapes – ordered by size; this is the first example of the acquisition of a complex hierarchical structure by a non-human primate and has been cited by Hauser and McDermott as a possible exception to the claim that only humans have "infinite productivity". McGonigle, Brendan. Putting Descartes before the horse. Behavioral and Brain Sciences. Vol 31 Apr 2008, 142-143. Warren, J. M. Effects of differential and nondifferential reinforcement on generalization test performance by cats. Journal of Comparative and Physiological Psychology. Vol 69 Dec 1969, 709-712. McGonigle, Brendan. Ordering and executive functioning as a window on the evolution and development of cognitive systems.
International Journal of Comparative Psychology. Vol 19 2006, 241-267. McGonigle, Brendan. Concurrent disjoint and reciprocal classification by Cebus apella in seriation tasks: Evidence for hierarchical organization. Animal Cognition. Vol 6 Sep 2003, 185-197. De Lillo, Carlo; the logic of searches in young children and tufted Capuchin-monkeys. International Journal of Comparative Psychology. Vol 10 1997, 1-24. Terrace, H. S. Memory and representation of serial order by children and pigeons. Current Directions in Psychological Science. Vol 3 Dec 1994, 180-189. Harris, M. R. A model of transitive choice; the Quarterly Journal of Experimental Psychology B: Comparative and Physiological Psychology. Vol 47B Aug 1994, 319-348. McGonigle, Brendan. Monkeys are rational! The Quarterly Journal of Experimental Psychology B: Comparative and Physiological Psychology. Vol 45B Oct 1992, 189-228. McGonigle, Brendan O. Non-verbal thinking by animals? Nature. Vol 325 Jan 1987, 110-112
Cytochrome c peroxidase, or CCP, is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome c and reduces hydrogen peroxide to water: CCP + H2O2 + 2 ferrocytochrome c + 2H+ → CCP + 2H2O + 2 ferricytochrome cCCP can be derived from aerobically grown yeast strains and can be isolated in both native and recombinant forms with high yield from Saccharomyces cerevisiae. The enzyme’s primary function is to eliminate toxic radical molecules produced by the cell which are harmful to biological systems, it works to maintain low concentration levels of hydrogen peroxide, generated by the organism through incomplete oxygen reduction. When glucose levels in fast growing yeast strains are exhausted, the cells turn to respiration which raises the concentration of mitochondrial H2O2. In addition to its peroxidase activity, it acts as a sensor and a signaling molecule to exogenous H2O2, which activates mitochondrial catalase activity. In eukaryotes, CCP contain a mono-b-type haem cofactor and is targeted to the intermembrane space of the mitochondria.
In prokaryotes, CCP is localized to the periplasm of the cell. Both enzymes work to resist peroxide-induced cellular stress. CCP plays an integral role in enabling inter-protein biological electron transfer; the negative charge transfer process is carried out by a complex formed between cytochrome c and cytochrome c peroxidase which occurs in the inter-membrane space of mitochondria. The mechanism involves ferrous cytochrome c providing electrons for the Cc-CcP system to reduce hydrogen peroxide to water; the complex is formed via disulfide bonds. Cytochrome c peroxidase can react with hydroperoxides other than hydrogen peroxide, but the reaction rate is much slower than with hydrogen peroxide, it was first isolated from baker's yeast by R. A. Altschul and Hogness in 1940, though not to purity; the first purified preparation of yeast CCP dates to Takashi Yonetani and his preparation by ion exchange chromatography in the early 1960s. The X-ray structure was coworkers in the late 1970s. CCP is the first heme enzyme to have its structure solved through X-ray crystallography.
The yeast enzyme is a monomer of molecular weight 34,000, containing 293 amino acids, contains as well a single non-covalently bound heme b. It is a moderately-sized enzyme; the apoenzyme, not active and bound to substrates, has an acidic isolelectric point of pH 5.0-5.2. Unusual for proteins, this enzyme crystallizes. More so, the enzyme purifies as a consequence of crystallization, making cycles of crystallization an effective final purification step. Much like catalase, the reaction of cytochrome c peroxidase proceeds through a three-step process, forming first a Compound I and a Compound II intermediate: CCP + ROOH → Compound I + ROH + H2O CCP-compound I + e− + H+ → Compound II Compound II + e− + H+ → CCP CCP in the resting state has a ferric heme, after the addition of two oxidizing equivalents from a hydroperoxide, it becomes oxidised to a formal oxidation state of +5 (FeV referred to as ferryl heme. However, both low-temperature magnetic susceptibility measurements and Mössbauer spectroscopy show that the iron in Compound I of CCP is a +4 ferryl iron, with the second oxidising equivalent existing as a long-lived free-radical on the side-chain of the tryptophan residue.
In its resting state, the Fe atom in the CCP heme is paramagnetic with high spin. Once the catalytic cycle is initiated, the iron atom is oxidized to form an oxyferryl intermediate has low spin; this is different from most peroxidases, which have the second oxidising equivalent on the porphyrin instead. Compound I of CCP is long-lived, decaying to CCP-compound II with a half-life at room temperature of 40 minutes to a couple hours. CCP has high sequence identity to the related ascorbate peroxidase enzyme. Amino acid analyzer studies reveal presence of residues of Asp, Ser, Pro, Ala, Met, Leu, Phe, His, Arg and Trp in crystalline CCP; the enzyme shows an unusual amino acid pattern compared to other peroxidase. Plant peroxidase such as horseradish peroxidase and pineapple peroxidase B have low lysine and tyrosine contents and high cysteine content. In contrast, CCP has high lysine and tyrosine content and low cysteine content; the enzyme contains a 68-residue sequence at the N-terminus of its monomeric protein, which targets it to the inter-membrane space of the mitochondria where it can the complex with cytochrome c and where it carries out its sensor and catalytic roles.
Studies indicate the distal arginine, a conserved amino acid among peroxidase, plays an important role in the catalytic activity of CCP by controlling its active site through stabilization of the reactive oxyferryl intermediate from control of its access. Cytochrome c peroxidase, maintained by the Kraut Research Group; the UniProt entry for yeast cytochrome c peroxidase