Review

for exam 2

Metabolism: Deni&on The totality of an organisms chemical reac3ons is called metabolism Types with examples: Catabolism and Anabolism *Catabolism: release energy by breaking down complex molecules to simpler compounds. A major pathway of catabolism is cellular respira3on, in which the sugar glucose and other organic fuels are broken down in the presence of oxygen to carbon dioxide and water. *Anabolism: consume energy to build complicated molecules from simpler ones; they are some3mes called biosynthe3c pathways. Examples of anabolism are the synthesis of an amino acid from simpler molecules and the synthesis of a protein from amino acids. Examples of exergonic, endergonic, spontaneous and non-spontaneous processes *spontaneous: energe3cally favorable A process that can occur without an input of energy is called a spontaneous process. explosion may be virtually instantaneous, while others, such as the rus3ng of an old car over 3me, are much slower. nonspontaneous: a process that cannot occur on its own, it will happen only if energy is added to the system. a bicycle cant work if you do not petal it. An exergonic reac3on proceeds with a net release of free energy An endergonic reac3on is one that absorbs free energyfrom its surroundings Gibbs equa&on and what does each term mean? G= H - T(S) This equa3on uses only proper3es of the system (the reac3on) itself: H symbolizes the change in the systems enthalpy (in biological systems, equivalent to total energy); S is the change in the systems entropy; and T is the absolute temperature in Kelvin (K) units State the two laws of thermodynamics rst law- Energy can be transferred and transformed, but it cannot be created or destroyed second law- Every energy transfer or transforma3on increases the entropy of the universe and during energy transfer, some amount of energy becomes unavailable, gets converted to heat. Bioenerge&cs: biology that concerns energy ow through living organisms Energy currency of the cell and its cycle Enzymes: biological catalyst

Lock and key, induced t with diagram Lock and key- ts perfectly induced t- ac3ve site changes Ac&va&on energy and lowering of reac&on temperature The eect of an enzyme on ac3va3on energy. Without aec3ng the free-energy change (G) for a reac3on, an enzyme speeds the reac3on by reducing its ac3va3on energy (EA). Above that temperature,however, the speed of the enzyma3c reac3on drops sharply. The thermal agita3on of the enzyme molecule disrupts the hydrogen bonds, ionic bonds, and other weak interac3ons that stabilize the ac3ve shape of the enzyme, and the protein molecule eventually denatures. Each enzyme has an op3mal temperature at which its reac3on rate is greatest. Without denaturing the enzyme, this temperature allows the greatest number of molecular collisions and the fastest conversion the reactants to product molecules. Most human enzymes have op3mal temperatures of about 3540C (close to human body temperature). The thermophilic bacteria that live in hot springs contain enzymes with op3mal temperatures 70C or higher Apoenzyme, Cofactor, coenzyme Many enzymes require nonprotein helpers for cataly3c ac3vity. These adjuncts, called cofactors, may be bound 3ghtly to the enzyme as permanent residents, or they may bind loosely and reversibly along with the substrate. The cofactors of some enzymes are inorganic, such as the metal atoms zinc, iron, and copper in ionic form. If the cofactor is an organic molecule, it is more specically called a coenzyme. Most vitamins are important in nutri3on because they act as coenzymes or raw materials from which coenzymes are made. Cofactors func3on in various ways, but in all cases where they. For a process to occur spontaneously, it must increase the entropy of the universe are used, they perform a crucial chemical func3on in catalysis. polypep3de or protein part of othe enzyme- apoenzyme