Brock Biology of Microorganisms (14th Edition)
14th Edition
ISBN: 9780321897398
Author: Michael T. Madigan, John M. Martinko, Kelly S. Bender, Daniel H. Buckley, David A. Stahl, Thomas Brock
Publisher: PEARSON
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Chapter 20.4, Problem 1MQ
Is H2S a substrate or a product of the sulfate-reducing bacteria? Of the chemolithotrophic sulfur bacteria?
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Chapter 20 Solutions
Brock Biology of Microorganisms (14th Edition)
Ch. 20.1 - How is new organic matter made in nature?Ch. 20.1 - In what ways are oxygenic photosynthesis and...Ch. 20.1 - What is a methane hydrate?Ch. 20.2 - Why does Syntrophomonas need a partner organism in...Ch. 20.2 - Prob. 2MQCh. 20.2 - What is the final product of acetogenesis?Ch. 20.3 - What is nitrogen fixation and why is it important...Ch. 20.3 - Prob. 2MQCh. 20.3 - How does the compound nitrapyrin benefit both...Ch. 20.4 - Is H2S a substrate or a product of the...
Ch. 20.4 - Prob. 2MQCh. 20.4 - Prob. 3MQCh. 20.5 - In what oxidation state is Fe in Fe(OH)3? In FeS?...Ch. 20.5 - Prob. 2MQCh. 20.5 - Why is excreted organic matter important to many...Ch. 20.6 - How does the formation of CaCO3 skeletons by...Ch. 20.6 - Prob. 2MQCh. 20.7 - What forms of mercury are most toxic to organisms?Ch. 20.7 - Prob. 2MQCh. 20.8 - What is the greenhouse effect and what causes it?Ch. 20.8 - What is the fate of most nitrogen used in...Ch. 20.8 - Why are the OMZs expanding and what are the likely...Ch. 20 - Prob. 1RQCh. 20 - Prob. 2RQCh. 20 - The principal form of nitrogen on Earth is N2,...Ch. 20 - Prob. 4RQCh. 20 - Prob. 5RQCh. 20 - Prob. 6RQCh. 20 - Prob. 7RQCh. 20 - Prob. 8RQCh. 20 - Compare and contrast the carbon, sulfur, and...Ch. 20 - 14C-labeled cellulose is added to a vial...Ch. 20 - Prob. 3AQ
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- With reference to their absorption spectra of the oxy haemoglobin intact line) and deoxyhemoglobin (broken line) shown in Figure 2 below, how would you best explain the reason why there are differences in the major peaks of the spectra? Figure 2. SPECTRA OF OXYGENATED AND DEOXYGENATED HAEMOGLOBIN OBTAINED WITH THE RECORDING SPECTROPHOTOMETER 1.4 Abs < 0.8 06 0.4 400 420 440 460 480 500 520 540 560 580 600 nm 1. The difference in the spectra is due to a pH change in the deoxy-haemoglobin due to uptake of CO2- 2. There is more oxygen-carrying plasma in the oxy-haemoglobin sample. 3. The change in Mr due to oxygen binding causes the oxy haemoglobin to have a higher absorbance peak. 4. Oxy-haemoglobin is contaminated by carbaminohemoglobin, and therefore has a higher absorbance peak 5. Oxy-haemoglobin absorbs more light of blue wavelengths and less of red wavelengths than deoxy-haemoglobinarrow_forwardWith reference to their absorption spectra of the oxy haemoglobin intact line) and deoxyhemoglobin (broken line) shown in Figure 2 below, how would you best explain the reason why there are differences in the major peaks of the spectra? Figure 2. SPECTRA OF OXYGENATED AND DEOXYGENATED HAEMOGLOBIN OBTAINED WITH THE RECORDING SPECTROPHOTOMETER 1.4 Abs < 0.8 06 0.4 400 420 440 460 480 500 520 540 560 580 600 nm 1. The difference in the spectra is due to a pH change in the deoxy-haemoglobin due to uptake of CO2- 2. There is more oxygen-carrying plasma in the oxy-haemoglobin sample. 3. The change in Mr due to oxygen binding causes the oxy haemoglobin to have a higher absorbance peak. 4. Oxy-haemoglobin is contaminated by carbaminohemoglobin, and therefore has a higher absorbance peak 5. Oxy-haemoglobin absorbs more light of blue wavelengths and less of red wavelengths than deoxy-haemoglobinarrow_forwardWhich ONE of the following is FALSE regarding haemoglobin? It has two alpha subunits and two beta subunits. The subunits are joined by disulphide bonds. Each subunit covalently binds a haem group. Conformational change in one subunit can be transmitted to another. There are many variant ("mutant") forms of haemoglobin that are not harmful.arrow_forward
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